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5UJK

Malate dehydrogenase from Methylobacterium extorquens, complexed with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate 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 activity
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY12
AGLY80
AVAL99
AILE119
AASN121
AMET144
ALEU148
AHIS176
AHOH512
AHOH517
AHOH522
AGLN13
AHOH528
AHOH546
AHOH549
AHOH559
AHOH579
AHOH580
AHOH595
AHOH635
AHOH642
AHOH658
AILE14
AHOH712
AHOH726
APHE33
AASP34
AILE35
AVAL36
ATHR78
AALA79

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 402
ChainResidue
AGLU287
AGLU287
AHOH612
AHOH614
AHOH673
AHOH705
AHOH714

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 403
ChainResidue
AGLU166
AHOH510
AHOH607
AHOH646
AHOH663
AHOH728

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
AARG154
AARG252
AHOH574
AHOH727

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00487
ChainResidueDetails
AHIS176

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00487
ChainResidueDetails
AASP34
AARG83
AARG89
AASN96
AILE119
AASN121
AARG152
AGLY10

221051

PDB entries from 2024-06-12

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