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

6H9S

Crystal dimeric structure of Petrotoga mobilis lactate dehydrogenase with NADH

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 PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY9
AILE115
AASN117
ATHR140
AHIS172
ATHR228
AHOH507
AHOH513
AHOH521
AHOH523
AHOH533
AARG10
AHOH550
AHOH551
AHOH563
AHOH575
AVAL11
AASP32
ALEU33
ATHR74
AALA75
AGLY76
AILE95

site_idAC2
Number of Residues24
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY9
BARG10
BVAL11
BASP32
BLEU33
BTHR74
BALA75
BGLY76
BALA77
BALA78
BILE95
BILE115
BASN117
BTHR140
BHIS172
BTHR228
BHOH512
BHOH515
BHOH528
BHOH532
BHOH533
BHOH545
BHOH555
BHOH580

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGEHGDS
ChainResidueDetails
AILE169-SER175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
AHIS172
BHIS172

site_idSWS_FT_FI2
Number of Residues26
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR62
AGLY76
AGLN79
AARG85
AILE115
AASN117
ATHR140
AASP145
AARG150
AHIS165
ATHR228
BVAL11
BASP32
BTYR62
BGLY76
BGLN79
BARG85
BILE115
BASN117
BTHR140
BASP145
BARG150
BHIS165
BTHR228
AVAL11
AASP32

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
ChainResidueDetails
ATYR219
BTYR219

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon