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3D0O

Crystal structure of Lactate Dehydrogenase from Staphylococcus Aureus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
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
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic process
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
Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDT
ChainResidueDetails
AILE176-THR182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J
ChainResidueDetails
AHIS179
BHIS179

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J
ChainResidueDetails
AALA16
BALA16

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J
ChainResidueDetails
AASP38
AGLY83
ATHR232
BASP38
BGLY83
BTHR232

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ALYS43
BASN124
ATYR69
AGLN86
ASER105
AASN124
BLYS43
BTYR69
BGLN86
BSER105

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|Ref.4, ECO:0007744|PDB:3H3J
ChainResidueDetails
AARG92
ASER147
BARG92
BSER147

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.4, ECO:0007744|PDB:3H3J
ChainResidueDetails
AALA122
BALA122

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|Ref.3, ECO:0000305|Ref.4, ECO:0007744|PDB:3D4P, ECO:0007744|PDB:3H3J
ChainResidueDetails
AASP152
BASP152

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR223
BTYR223

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS179
AASP152

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS179
BASP152

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS179
AARG155
AASP152

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS179
BARG155
BASP152

227111

PDB entries from 2024-11-06

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