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6PBL

Crystal structure of Malate dehydrogenase from Legionella pneumophila Philadelphia 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0006108biological_processmalate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase 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
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006108biological_processmalate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. MTTLDelRArtqL
ChainResidueDetails
AMET156-LEU168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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