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

1MV8

1.55 A crystal structure of a ternary complex of GDP-mannose dehydrogenase from Psuedomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0006970biological_processresponse to osmotic stress
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0036460biological_processcellular response to cell envelope stress
A0042121biological_processalginic acid biosynthetic process
A0044010biological_processsingle-species biofilm formation
A0047919molecular_functionGDP-mannose 6-dehydrogenase activity
A0051287molecular_functionNAD binding
B0006970biological_processresponse to osmotic stress
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0036460biological_processcellular response to cell envelope stress
B0042121biological_processalginic acid biosynthetic process
B0044010biological_processsingle-species biofilm formation
B0047919molecular_functionGDP-mannose 6-dehydrogenase activity
B0051287molecular_functionNAD binding
C0006970biological_processresponse to osmotic stress
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0036460biological_processcellular response to cell envelope stress
C0042121biological_processalginic acid biosynthetic process
C0044010biological_processsingle-species biofilm formation
C0047919molecular_functionGDP-mannose 6-dehydrogenase activity
C0051287molecular_functionNAD binding
D0006970biological_processresponse to osmotic stress
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0036460biological_processcellular response to cell envelope stress
D0042121biological_processalginic acid biosynthetic process
D0044010biological_processsingle-species biofilm formation
D0047919molecular_functionGDP-mannose 6-dehydrogenase activity
D0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCNVWH
ChainResidueDetails
ATYR211-HIS217

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12705829
ChainResidueDetails
ACYS268
BCYS268
CCYS268
DCYS268

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: in chain A => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8
ChainResidueDetails
ATYR10
BLYS35
BTHR86
BTHR124
CTYR10
CVAL11
CASP30
CLYS35
CTHR86
CTHR124
DTYR10
AVAL11
DVAL11
DASP30
DLYS35
DTHR86
DTHR124
AASP30
ALYS35
ATHR86
ATHR124
BTYR10
BVAL11
BASP30

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: in chain A => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU
ChainResidueDetails
AGLU161
BASN225
CGLU161
CLYS210
CASN214
CHIS217
CASN225
DGLU161
DLYS210
DASN214
DHIS217
ALYS210
DASN225
AASN214
AHIS217
AASN225
BGLU161
BLYS210
BASN214
BHIS217

site_idSWS_FT_FI4
Number of Residues24
DetailsBINDING: in chain B => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU
ChainResidueDetails
ATYR256
BPHE262
BGLY265
BLYS324
CTYR256
CTYR257
CARG259
CPHE262
CGLY265
CLYS324
DTYR256
ATYR257
DTYR257
DARG259
DPHE262
DGLY265
DLYS324
AARG259
APHE262
AGLY265
ALYS324
BTYR256
BTYR257
BARG259

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: in chain B => ECO:0000269|PubMed:12705829, ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8
ChainResidueDetails
ALYS271
AARG331
BLYS271
BARG331
CLYS271
CARG331
DLYS271
DARG331

218196

PDB entries from 2024-04-10

PDB statisticsPDBj update infoContact PDBjnumon