Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AARG166

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP447

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon