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1D8C

MALATE SYNTHASE G COMPLEXED WITH MAGNESIUM AND GLYOXYLATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004474molecular_functionmalate synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0009436biological_processglyoxylate catabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00589
Number of Residues16
DetailsPTS_HPR_SER PTS HPR domain serine phosphorylation site signature. EIsLHgRSLLFIRnVG
ChainResidueDetails
AGLU326-GLY341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASN339

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AARG632

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AVAL119
ATYR126
AVAL275
ALYS312
AASN339
AGLU428
APHE453
AARG456
ASER537

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641, ECO:0000269|PubMed:12930982
ChainResidueDetails
ASER618
AALA689

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 20181690
ChainResidueDetails
AASP631
AARG338
AASP270
AGLU272

site_idMCSA1
Number of Residues6
DetailsM-CSA 53
ChainResidueDetails
ACYS271electrostatic stabiliser, hydrogen bond acceptor
AASP273electrostatic stabiliser, hydrogen bond acceptor
AASN339electrostatic stabiliser, hydrogen bond donor
AGLU428metal ligand
AARG456metal ligand
AARG632electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-10-30

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