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

6AOO

2.15 Angstrom Resolution Crystal Structure of Malate Dehydrogenase from Haemophilus influenzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
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
B0005737cellular_componentcytoplasm
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 PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 401
ChainResidue
AARG81
AARG153
AGLY210
AALA223
AMET227

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 402
ChainResidue
AHOH600
ATYR138
AASP139
ALYS140
AARG141

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 403
ChainResidue
ASER167
AARG168
AHOH552
BARG236

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
BARG153
BGLY210
BSER222
BALA223
BMET227

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 B 402
ChainResidue
BSER167
BARG168
BHOH565

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 B 403
ChainResidue
BLYS133
BGLY136
BVAL137
BTYR138
BHOH545
BHOH552

Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. VTTLDvlRSetfV
ChainResidueDetails
AVAL146-VAL158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS177
BHIS177

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY7
BGLY7
BASP34
BARG81
BARG87
BASN94
BILE117
BASN119
BARG153
BMET227
AASP34
AARG81
AARG87
AASN94
AILE117
AASN119
AARG153
AMET227

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon