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1EZ4

CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION

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
C0003824molecular_functioncatalytic activity
C0004459molecular_functionL-lactate dehydrogenase activity
C0005737cellular_componentcytoplasm
C0006089biological_processlactate metabolic process
C0006090biological_processpyruvate metabolic process
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
D0006089biological_processlactate metabolic process
D0006090biological_processpyruvate metabolic process
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 PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD A 1352
ChainResidue
AGLY29
AGLY97
AALA98
AILE116
ASER119
AALA136
AASN138
AVAL140
ASER161
ALEU165
AHIS193
AALA30
AHOH1427
AHOH1476
AHOH1527
AVAL31
AASP52
AVAL53
AARG57
ATYR83
ATHR95
AALA96

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 1353
ChainResidue
BASP28
BGLY29
BALA30
BVAL31
BASP52
BVAL54
BTHR95
BALA96
BGLY97
BILE116
BALA136
BALA137
BASN138
BVAL140
BSER161
BLEU165
BHIS193
BILE251
BHOH1457
BHOH1458
BHOH1471
BHOH1472
BHOH1544
BHOH1557

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD C 1354
ChainResidue
CASP28
CGLY29
CALA30
CVAL31
CASP52
CVAL53
CARG57
CTYR83
CTHR95
CALA96
CGLY97
CILE116
CSER119
CALA136
CASN138
CVAL140
CSER161
CHIS193
CILE251
CHOH1429
CHOH1528

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD D 1355
ChainResidue
DGLY29
DALA30
DVAL31
DASP52
DVAL53
DTHR95
DALA96
DGLY97
DILE116
DSER119
DALA136
DALA137
DASN138
DSER161
DLEU165
DHIS193
DILE251
DHOH1387
DHOH1452
DHOH1467
DHOH1468

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. MGEHGDS
ChainResidueDetails
AMET190-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:11807949, ECO:0000305|PubMed:1425707, ECO:0007744|PDB:1EZ4
ChainResidueDetails
AHIS193
BHIS193
CHIS193
DHIS193

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
AVAL31
BGLN100
BARG106
BASN138
BASP166
BTHR247
CVAL31
CTYR83
CGLN100
CARG106
CASN138
ATYR83
CASP166
CTHR247
DVAL31
DTYR83
DGLN100
DARG106
DASN138
DASP166
DTHR247
AGLN100
AARG106
AASN138
AASP166
ATHR247
BVAL31
BTYR83

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:11807949, ECO:0007744|PDB:1EZ4
ChainResidueDetails
AASP52
BSER119
BALA136
BSER161
CASP52
CARG57
CGLY97
CSER119
CALA136
CSER161
DASP52
AARG57
DARG57
DGLY97
DSER119
DALA136
DSER161
AGLY97
ASER119
AALA136
ASER161
BASP52
BARG57
BGLY97

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR238
BTYR238
CTYR238
DTYR238

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASP166
AHIS193

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASP166
BHIS193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CASP166
CHIS193

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DASP166
DHIS193

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS193
AASP166
AARG169

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS193
BASP166
BARG169

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
CHIS193
CASP166
CARG169

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
DHIS193
DASP166
DARG169

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PDB entries from 2024-07-17

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