1MO0

Structural Genomics Of Caenorhabditis Elegans: Triose Phosphate Isomerase

PDB DOI: https://doi.org/10.2210/pdb1MO0/pdb

Classification: ISOMERASE
Organism(s): Caenorhabditis elegans
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2002-09-06 Released: 2002-09-13
Deposition Author(s): Symersky, J., Li, S., Finley, J., Liu, Z.-J., Qui, H., Luan, C.H., Carson, M., Tsao, J., Johnson, D., Lin, G., Zhao, J., Thomas, W., Nagy, L.A., Sha, B., DeLucas, L.J., Wang, B.-C., Luo, M., Southeast Collaboratory for Structural Genomics (SECSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.213
R-Value Work: 0.183
R-Value Observed: 0.183

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Structural genomics of Caenorhabditis elegans: triosephosphate isomerase

Symersky, J., Li, S., Carson, M., Luo, M.

(2003) Proteins 51: 484-486

PubMed: 12696058 Search on PubMed
DOI: https://doi.org/10.1002/prot.10364
Primary Citation of Related Structures:
1MO0

Organizational Affiliation

Southeast Collaboratory for Structural Genomics, Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, 35294, USA.

Macromolecule Content

Total Structure Weight: 60.36 kDa
Atom Count: 4,294
Modelled Residue Count: 502
Deposited Residue Count: 550
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Triosephosphate isomerase	A, B	275	Caenorhabditis elegans	Mutation(s): 0 EC: 5.3.1.1
UniProt
Find proteins for Q10657 (Caenorhabditis elegans) Explore Q10657 Go to UniProtKB: Q10657
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q10657
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain D [auth A] SDF format, chain F [auth A] SDF format, chain I [auth B] SDF format, chain E [auth A] SDF format, chain H [auth B] MOL2 format, chain D [auth A] MOL2 format, chain F [auth A] MOL2 format, chain I [auth B] MOL2 format, chain E [auth A] MOL2 format, chain H [auth B]	D [auth A], E [auth A], F [auth A], H [auth B], I [auth B]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain H [auth B] Focus chain I [auth B] Interactions & Density Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain H [auth B] Focus chain I [auth B]
ACT Query on ACT Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain G [auth B] MOL2 format, chain C [auth A] MOL2 format, chain G [auth B]	C [auth A], G [auth B]	ACETATE ION C₂ H₃ O₂ QTBSBXVTEAMEQO-UHFFFAOYSA-M		Interactions Focus chain C [auth A] Focus chain G [auth B] Interactions & Density Focus chain C [auth A] Focus chain G [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.70 Å
R-Value Free: 0.213
R-Value Work: 0.183
R-Value Observed: 0.183
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 36.399	α = 90
b = 64.373	β = 91.53
c = 105.706	γ = 90

Software Package:

Software Name	Purpose
HKL-2000	data collection
HKL-2000	data reduction
SOLVE	phasing
RESOLVE	model building
CNS	refinement
HKL-2000	data scaling
RESOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2002-09-13

Deposition Author(s):

Southeast Collaboratory for Structural Genomics (SECSG)

Revision History (Full details and data files)

Version 1.0: 2002-09-13
Type: Initial release
Version 1.1: 2008-04-28
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-14
Changes: Data collection, Database references, Derived calculations
Version 1.4: 2024-04-03
Changes: Refinement description

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1MO0

Structural Genomics Of Caenorhabditis Elegans: Triose Phosphate Isomerase

Structural genomics of Caenorhabditis elegans: triosephosphate isomerase

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)