2QQ2

Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7

PDB DOI: https://doi.org/10.2210/pdb2QQ2/pdb

Classification: HYDROLASE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2007-07-26 Released: 2007-08-14
Deposition Author(s): Busam, R., Lehtio, L., Arrowsmith, C.H., Berglund, H., Collins, R., Dahlgren, L.G., Herman, M.D., Edwards, A., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Hallberg, B.M., Holmberg-Schiavone, L., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Moche, M., Nordlund, P., Nyman, T., Sagemark, J., Stenmark, P., Sundstrom, M., Thorsell, A.G., Tresaugues, L., van den Berg, S., Weigelt, J., Welin, M., Persson, C., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.239
R-Value Work: 0.216
R-Value Observed: 0.217

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Human acyl-CoA thioesterase 7.

Busam, R., Lehtio, L., Arrowsmith, C.H., Berglund, H., Collins, R., Dahlgren, L.G., Herman, M.D., Edwards, A., Flodin, S., Flores, A., Greslund, S., Hammarstrom, M., Hallberg, B.M., Holmberg-Schiavone, L., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Moche, M., Nordlund, P., Nyman, T., Sagemark, J., Stenmark, P., Sundstrom, M., Thorsell, A.G., Tresaugues, L., van den Berg, S., Weigelt, J., Welin, M., Persson, C.

To be published.

Macromolecule Content

Total Structure Weight: 256.67 kDa
Atom Count: 14,037
Modelled Residue Count: 1,829
Deposited Residue Count: 2,316
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Cytosolic acyl coenzyme A thioester hydrolase	A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	193	Homo sapiens	Mutation(s): 0 Gene Names: ACOT7, BACH EC: 3.1.2.2
UniProt & NIH Common Fund Data Resources
Find proteins for O00154 (Homo sapiens) Explore O00154 Go to UniProtKB: O00154
PHAROS: O00154 GTEx: ENSG00000097021
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O00154
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.239
R-Value Work: 0.216
R-Value Observed: 0.217
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 80.95	α = 79.61
b = 81.6	β = 89.7
c = 105.1	γ = 74.12

Software Package:

Software Name	Purpose
REFMAC	refinement
ProDC	data collection
XDS	data reduction
XSCALE	data scaling
BALBES	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-08-14

Deposition Author(s):

Holmberg-Schiavone, L.

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2007-08-14
Type: Initial release
Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.2: 2023-08-30
Changes: Data collection, Database references, Refinement description

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Help and Resources

2QQ2

Crystal structure of C-terminal domain of Human acyl-CoA thioesterase 7

Human acyl-CoA thioesterase 7.

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)