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3TL2

Crystal structure of Bacillus anthracis str. Ames malate dehydrogenase in closed conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase (NAD+) activity
A0006089biological_processlactate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 313
ChainResidue
AARG87
AMET91
AARG93
ALEU96
APRO126

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 314
ChainResidue
APRO126
AVAL127
AASP128
AHOH676

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 315
ChainResidue
AILE11
AASP36
ATYR70
AILE107
AHOH481
AHOH589

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN A 316
ChainResidue
ALYS283
AHOH512
AHOH592

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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