Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5YTA

Pig Heart Lactate Dehydrogenase in complex with NADH and Oxamate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic 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
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic 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 PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY30
AVAL99
AARG100
AVAL117
AILE121
AVAL137
ASER138
AASN139
ASER162
ALEU166
AHIS194
AGLN31
ATHR249
AILE253
AOXM402
AHOH506
AHOH520
AHOH521
AHOH533
AHOH534
AHOH536
AHOH545
AVAL32
AHOH547
AHOH566
AASP53
AVAL54
ALEU55
ATHR96
AALA97
AGLY98

site_idAC2
Number of Residues8
Detailsbinding site for residue OXM A 402
ChainResidue
AGLN101
AARG107
AASN139
AARG170
AHIS194
AALA239
ATHR249
ANAD401

site_idAC3
Number of Residues29
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY30
BGLN31
BVAL32
BASP53
BVAL54
BLEU55
BTHR96
BALA97
BGLY98
BVAL99
BARG100
BVAL117
BVAL137
BSER138
BASN139
BSER162
BLEU166
BHIS194
BTHR249
BILE253
BOXM402
BHOH501
BHOH504
BHOH509
BHOH510
BHOH515
BHOH524
BHOH540
BHOH551

site_idAC4
Number of Residues9
Detailsbinding site for residue OXM B 402
ChainResidue
BGLN101
BARG107
BASN139
BLEU166
BARG170
BHIS194
BALA239
BTHR249
BNAD401

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. LGEHGDS
ChainResidueDetails
ALEU191-SER197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS194
BHIS194

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG107
AASN139
AARG170
ATHR249
BGLY30
BARG100
BARG107
BASN139
BARG170
BTHR249
AGLY30
AARG100

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:838465
ChainResidueDetails
BALA2
AALA2

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07195
ChainResidueDetails
ALYS119
ALYS329
BLYS7
BLYS58
BLYS119
BLYS329
ALYS7
ALYS58

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07195
ChainResidueDetails
BSER44
ASER44

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07195
ChainResidueDetails
ATYR240
BTYR240

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon