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3VPH

L-lactate dehydrogenase from Thermus caldophilus GK24 complexed with oxamate, NADH and FBP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase activity
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0019752biological_processcarboxylic acid metabolic process
D0003824molecular_functioncatalytic activity
D0004459molecular_functionL-lactate dehydrogenase activity
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0019752biological_processcarboxylic acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU190-SER196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:25258319
ChainResidueDetails
AHIS193
BHIS193
CHIS193
DHIS193

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25258319, ECO:0007744|PDB:3VPH
ChainResidueDetails
AMET30
BMET30
CMET30
DMET30

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:25258319, ECO:0007744|PDB:3VPH
ChainResidueDetails
AASP52
BALA136
BSER161
BARG171
CASP52
CTYR83
CGLY97
CALA136
CSER161
CARG171
DASP52
ATYR83
DTYR83
DGLY97
DALA136
DSER161
DARG171
AGLY97
AALA136
ASER161
AARG171
BASP52
BTYR83
BGLY97

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
AGLN100
AARG106
BGLN100
BARG106
CGLN100
CARG106
DGLN100
DARG106

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:25258319, ECO:0007744|PDB:3VPH
ChainResidueDetails
AASN138
DASN138
DASP166
DTHR247
AASP166
ATHR247
BASN138
BASP166
BTHR247
CASN138
CASP166
CTHR247

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:25258319, ECO:0007744|PDB:3VPH
ChainResidueDetails
AGLN183
BGLN183
CGLN183
DGLN183

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR238
BTYR238
CTYR238
DTYR238

222415

PDB entries from 2024-07-10

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