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3CV1

Atomic Resolution Structures of Escherichia coli and Bacillis anthracis Malate Synthase A: Comparison with Isoform G and Implications for Structure Based Drug Design

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004474molecular_functionmalate synthase activity
A0005737cellular_componentcytoplasm
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AGLN53
AGLN56
AHOH684
AHOH718
AHOH814

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 534
ChainResidue
AHOH688
AHOH971
AGLU250
AASP278
AHOH541
AHOH657

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 535
ChainResidue
APHE13
ATYR17
AHOH870
AHOH987

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 536
ChainResidue
AILE73
ATRP219
AHIS263
AALA264
AHOH784
AHOH907

Functional Information from PROSITE/UniProt
site_idPS00510
Number of Residues16
DetailsMALATE_SYNTHASE Malate synthase signature. RDHivGLNcGrWDYIF
ChainResidueDetails
AARG266-PHE281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d8c
ChainResidueDetails
AARG166
AASP117
AASP447
AGLU119

238582

PDB entries from 2025-07-09

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