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

6IHE

Crystal structure of Malate dehydrogenase from Metallosphaera sedula

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004459molecular_functionL-lactate dehydrogenase activity
A0006089biological_processlactate metabolic process
A0006090biological_processpyruvate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004459molecular_functionL-lactate dehydrogenase activity
B0006089biological_processlactate metabolic process
B0006090biological_processpyruvate metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY10
AGLY79
ALYS80
APRO81
AVAL118
AASN120
AVAL144
ATHR218
AMLT402
AHOH509
AHOH515
ALYS11
AHOH532
AHOH553
AHOH560
AHOH563
AILE12
ATYR32
AASP33
AILE34
AILE35
ASER77
AALA78

site_idAC2
Number of Residues11
Detailsbinding site for residue MLT A 402
ChainResidue
AARG82
AARG88
AASN120
AARG148
AHIS172
APRO208
AILE212
ATHR218
ANAD401
AHOH509
AHOH560

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 403
ChainResidue
ALYS131
ATYR132
ALYS134
AGLU250
AHOH507

site_idAC4
Number of Residues3
Detailsbinding site for residue PGE A 404
ChainResidue
AASP27
AASN58
AHOH526

site_idAC5
Number of Residues6
Detailsbinding site for residue PGE A 405
ChainResidue
APHE167
ATHR182
ALEU273
AHOH580
BGLY267
BPRO268

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
ASER19
AVAL22
ASER23
ALYS53
AHOH504

site_idAC7
Number of Residues4
Detailsbinding site for residue PG4 A 407
ChainResidue
AASP72
AGLY112
AHOH568
BLYS186

site_idAC8
Number of Residues6
Detailsbinding site for residue PG4 A 408
ChainResidue
ATHR162
ASER163
ALYS186
BASP72
BGLY112
BPGE405

site_idAC9
Number of Residues1
Detailsbinding site for residue PEG A 409
ChainResidue
AGLU276

site_idAD1
Number of Residues30
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY10
BLYS11
BILE12
BTYR32
BASP33
BILE34
BILE35
BLEU38
BSER77
BALA78
BGLY79
BLYS80
BPRO81
BASN95
BILE98
BVAL118
BALA119
BASN120
BVAL144
BTHR218
BPRO222
BMLT402
BHOH502
BHOH503
BHOH515
BHOH530
BHOH534
BHOH538
BHOH571
BHOH578

site_idAD2
Number of Residues8
Detailsbinding site for residue MLT B 402
ChainResidue
BTHR218
BNAD401
BHOH502
BARG82
BARG88
BASN120
BARG148
BILE212

site_idAD3
Number of Residues5
Detailsbinding site for residue GOL B 403
ChainResidue
ALYS231
AGLU237
BLYS231
BGLU237
BHOH565

site_idAD4
Number of Residues4
Detailsbinding site for residue PGE B 404
ChainResidue
AASP40
ALYS41
AILE207
BLYS251

site_idAD5
Number of Residues8
Detailsbinding site for residue PGE B 405
ChainResidue
ALYS186
AGLY187
APG4408
BGLY112
BPHE136
BSER264
BSER265
BILE266

site_idAD6
Number of Residues2
Detailsbinding site for residue PGE B 406
ChainResidue
BSER108
BLYS109

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO B 407
ChainResidue
BTRP280
BASN283
BSER284
BLYS287

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO B 408
ChainResidue
BPHE167
BTHR182
BHOH501

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO B 409
ChainResidue
BSER19
BVAL22
BSER23
BLYS53

site_idAE1
Number of Residues3
Detailsbinding site for residue PEG B 410
ChainResidue
BGLU199
BASP202
BHOH582

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon