2VKT

HUMAN CTP SYNTHETASE 2 - GLUTAMINASE DOMAIN

PDB DOI: https://doi.org/10.2210/pdb2VKT/pdb

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

Deposited: 2007-12-28 Released: 2008-01-15
Deposition Author(s): Welin, M., Tresaugues, L., Arrowsmith, C.H., Berglund, H., Busam, R.D., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Herman, M.D., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Lehtio, L., Moche, M., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Svensson, L., Thorsell, A.G., van den Berg, S., Weigelt, J., Nordlund, P., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.239
R-Value Work: 0.207
R-Value Observed: 0.209

wwPDB Validation 3D Report Full Report

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

Literature

Human Ctp Synthetase 2 - Glutaminase Domain

Welin, M., Tresaugues, L., Arrowsmith, C.H., Berglund, H., Busam, R.D., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Herman, M.D., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Lehtio, L., Moche, M., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Svensson, L., Thorsell, A.G., Van Den Berg, S., Weigelt, J., Nordlund, P.

To be published.

Macromolecule Content

Total Structure Weight: 32.62 kDa
Atom Count: 2,047
Modelled Residue Count: 252
Deposited Residue Count: 289
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
CTP SYNTHASE 2	A	289	Homo sapiens	Mutation(s): 0 EC: 6.3.4.2
UniProt & NIH Common Fund Data Resources
Find proteins for Q9NRF8 (Homo sapiens) Explore Q9NRF8 Go to UniProtKB: Q9NRF8
PHAROS: Q9NRF8 GTEx: ENSG00000047230
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9NRF8
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.239
R-Value Work: 0.207
R-Value Observed: 0.209
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 105.2	α = 90
b = 73.1	β = 95.6
c = 50.5	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling
MOLREP	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-01-15

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2008-01-15
Type: Initial release
Version 1.1: 2015-04-29
Changes: Derived calculations, Non-polymer description, Other, Source and taxonomy, Version format compliance
Version 1.2: 2023-12-13
Changes: Data collection, Database references, Other, Refinement description

Prepare Data

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Deposit Data

Help and Resources

2VKT

HUMAN CTP SYNTHETASE 2 - GLUTAMINASE DOMAIN

Human Ctp Synthetase 2 - Glutaminase Domain

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)