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3LDH

A comparison of the structures of apo dogfish m4 lactate dehydrogenase and its ternary complexes

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues34
DetailsBINDING SITE FOR RESIDUE NAD A 332
ChainResidue
AVAL27
AGLU56
AASP57
ALYS58
ALEU59
ALYS60
AGLU62
ASER80
AGLY81
ALYS83
AASP84
AGLY28
ATYR85
ATYR85
ATHR97
AALA98
AGLY99
AARG101
ALEU137
AHIS138
APRO139
AGLU140
ACYS29
ASER163
AHIS195
ATYR246
AALA248
APYR333
AASP30
AASP30
AASP53
AVAL54
AMET55
AMET55

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PYR A 333
ChainResidue
ALEU167
AARG171
AHIS195
ANAD332

Functional Information from PROSITE/UniProt
site_idPS00064
Number of Residues7
DetailsL_LDH L-lactate dehydrogenase active site. IGQHGDS
ChainResidueDetails
AILE192-SER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AGLY196

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:3430615
ChainResidueDetails
AALA31
AGLN102

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALEU110
ALEU141
ATHR229

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING:
ChainResidueDetails
APHE172

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:838743
ChainResidueDetails
AALA2

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 584
ChainResidueDetails
ALEU110electrostatic stabiliser
ASER169enhance reactivity
APHE172electrostatic stabiliser
AGLY196proton acceptor, proton donor

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PDB entries from 2024-04-24

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