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2X0J

2.8 A RESOLUTION STRUCTURE OF MALATE DEHYDROGENASE FROM ARCHAEOGLOBUS FULGIDUS IN COMPLEX WITH ETHENO-NAD

Replaces:  1OJU
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ENA A 1000
ChainResidue
AGLY30
AGLY99
AILE119
AVAL138
AASN140
AMET142
AMET163
ALEU167
AHIS195
ATHR246
APRO250
AARG31
ASO42000
AHOH2029
AHOH2030
AVAL32
AASP53
AILE54
ALEU58
ATYR85
ATHR97
AALA98

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2000
ChainResidue
AASN140
ALEU167
AARG171
AHIS195
AALA236
ATHR246
AENA1000

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDS
ChainResidueDetails
AILE192-SER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AHIS195

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14659762
ChainResidueDetails
AGLY28
AASP53
AASN116
AVAL138

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AARG102
AARG109
AASN140
AARG171

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AASP168

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS195
AARG171
AASP168

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PDB entries from 2024-07-17

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