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9END

Crystal structure of Methanopyrus kandleri malate dehydrogenase mutant 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0006089biological_processlactate 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
A0046554molecular_functionL-malate dehydrogenase (NADP+) activity
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
B0006089biological_processlactate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
B0046554molecular_functionL-malate dehydrogenase (NADP+) activity
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDT
ChainResidueDetails
AILE175-THR181

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AHIS178
BHIS178

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q60176
ChainResidueDetails
AGLY8
AASN98
AVAL121
BGLY8
BASN98
BVAL121

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P61889
ChainResidueDetails
AGLN85
AARG91
AASN123
AARG154
BGLN85
BARG91
BASN123
BARG154

237992

PDB entries from 2025-06-25

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