PSI TargetDB

Statistics Summary Report for CHTSB Center

Last updated: Feb 2 2012



Target Status Statistics

Total number of targets deposited by CHTSB to TargetDB: 129

      View CHTSB Target List

Table 1: Status Statistics for CHTSB

Status Total Number of Targets(%) Relative to "Cloned" Targets(%) Relative to "Expressed" Targets(%) Relative to "Purified" Targets(%) Relative to "Crystallized" Targets
Cloned129100.0---
Expressed3426.4100.0--
Soluble1612.447.1--
Purified1612.447.1100.0-
Crystallized75.420.643.8100.0
Diffraction-quality Crystals53.914.731.271.4
Diffraction53.914.731.271.4
NMR Assigned00.00.00.0-
HSQC00.00.00.0-
Crystal Structure53.914.731.271.4
NMR Structure00.00.00.0-
In PDB153.914.731.271
Work Stopped40----
Test Target0----
Other0----

Last updated: Feb 2 2012


Note 1:   Number of targets with status "in PDB" may not be equal to number of structures determined by a project. A target may reference several PDB IDs (example: structure of the same polypeptides with different ligands). Multiple targets in TargetDB may identify the same PDB structure when a stucture is a result of collaboration between different centers and each center includes the target on its target list.

Table 2: Status Statistics for CHTSB by Organism

These statistics are derived from mapping of target sequences to GenBank using >=98% sequence identity cut off.


Organism Total Number1 Work Stopped Cloned Expressed Purified Crystallized Crystal Structure NMR Structure In PDB
Yeast1254012530123101
Eukaryota1294012934167505
Uncultured or unidentified101000000

Last updated: Feb 2 2012

Note 1:   Total counts in this table may differ from total number of targets and structures. A target is counted in different organism specifications if:
- a target is mapped to different organisms
- a target is a hybrid complex (for example:a complex of human and mouse polypeptides).

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Deposited Structure Statistics for CHTSB Center

Number of Released X-Ray Structures: 13

Number of Released NMR Structures: 3

Total number of released structures from CHTSB center in the PDB: 16

Table 3: PDB Status Statistics for Structures from CHTSB

PDB StatusNumber of Structures
Total Deposited16
Released16
In Process0
Last updated: Feb 2 2012
Note 1:   "Total Deposited" are all structures in the PDB including structures released to the public and structures that are in the process to be released ("Released on Publication" , "Released on Certain Date", etc.).

Table 4: List of Structures Deposited in the PDB by CHTSB

Total number of structures: 16

Structures of distinct targets: 161

1   A target may reference several PDB IDs (example: structure of the same polypeptides with different ligands).
In this case only one structure is counted to compute number of structures of distinct targets.

Related PDB_ID(s): PDB_ID(s) associated with the same target in TargetDB.

PDB_ID TitleTarget_id Deposition DateReleased Date PDB StatusRelated PDB_ID in TargetDB
2VDU structure of trm8, m7g methylation enzymeCX000312007-10-112007-12-18RELnone
1AYZ crystal structure of the saccharomyces cerevisiae ubiquitin-conjugating enzyme rad6 (ubc2) at 2.6a resolutionCX000291997-11-121998-08-26RELnone
3JW1 crystal structure of bovine pancreatic ribonuclease complexed with uridine-5'-monophosphate at 1.60 a resolutionTAR3JW12009-09-172009-10-06RELnone
2QCA a new crystal form of bovine pancreatic rnase a in complex with 2'-deoxyguanosine-5'-monophosphateTAR2QCA2007-06-192007-07-03RELnone
3DYB proteinase k- digalacturonic acid complexTAR3DYB2008-07-252008-10-07RELnone
3ENJ structure of pig heart citrate synthase at 1.78 a resolutionTAR3ENJ2008-09-252009-02-03RELnone
2J6A crystal structure of s. cerevisiae ynr046w, a zinc finger protein from the erf1 methyltransferase complex.CX00045 CHTSB:CX00046 CHTSB:CX00048 CHTSB:CX000502006-09-272006-09-28RELnone
1Q67 crystal structure of dcp1pCX000092003-08-122004-03-02RELnone
2AXQ apo histidine-tagged saccharopine dehydrogenase (l-glu forming) from saccharomyces cerevisiaeCX00047 CHTSB:CX00049 CHTSB:CX000512005-09-052006-08-15RELnone
1HV2 solution structure of yeast elongin c in complex with a von hippel-lindau peptideCX000362001-01-052001-09-06RELnone
2IP1 crystal structure analysis of s. cerevisiae tryptophanyl trna synthetaseYOL097C2006-10-112007-06-26RELnone
2FA4 crystal structure of oxidized form from saccharomyces cerevisiaeCX000442005-12-062006-12-06RELnone
3BTS crystal structure of a ternary complex of the transcriptional repressor gal80p (gal80s0 [g301r]) and the acidic activation domain of gal4p (aa 854-874) from saccharomyces cerevisiae with nadCX00015 CHTSB:CX000162007-12-302008-03-04RELnone
2I9H nmr solution structure of the reduced form of thioredoxin 1 from yeast (trx1)CX000432006-09-052007-07-17RELnone
1YOP the solution structure of kti11pCX00033 CHTSB:CX000342005-01-282005-04-05RELnone
1BOB histone acetyltransferase hat1 from saccharomyces cerevisiae in complex with acetyl coenzyme aCX000211998-07-021999-04-20RELnone

Last updated: Feb 2 2012

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Sequence Redundancy Statistics

Table 5: Sequence Redundancy Statistics for CHTSB by Experimental Status

Sequence Identity(%)Novel Targets
Status:
Selected
Novel Targets
Status:
Cloned
Novel Targets
Status:
Expressed
Novel Targets
Status:
Purified
Novel Targets
Status:
Crystallized
Novel Targets
Status:
Crystal Structure
Novel Targets
Status:
in PDB
<1001671673820644
<981671673820644
<951671673820644
<901671673820644
<701641643720644
<501611613720644
<401551593720644
<301101263520644
Last updated: 12-01-10
Sequence redundancy is calculated by clustering analysis using BLASTClust program with similarity threshold set to percent of sequence identity.   Please view detailed explanation of sequence redundancy calculations and BLASTClust threshold settings.  Sequence redundancy calculations are based on comparison to all protein sequences in TargetDB which are in the same experimental status category and at least 20 amino acids long.

Table 6: Sequence Redundancy Statistics for Structures Released by CHTSB by Year

Year Released Structures Number of Released Structures <30% Identity at Time of Release Percent(%) of Released Structures <30% Identity(%) at Time of Release
2001100
200411100
2005100
20063133
20074125
20082150
2009200
Total16531
Last updated: 12-02-02
Sequence redundancy is calculated by clustering analysis using BLASTClust program with similarity threshold set to percent of sequence identity.   Please view detailed explanation of sequence redundancy calculations and BLASTClust threshold settings.  Sequence redundancy calculations are based on comparison to all protein sequences in the PDB which are at least 20 amino acids long.
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