Structure of PDB 1mv8 Chain D

Receptor sequence
>1mv8D (length=436) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
MRISIFGLGYVGAVCAGCLSARGHEVIGVDVSSTKIDLINQGKSPIVEPG
LEALLQQGRQTGRLSGTTDFKKAVLDSDVSFICVGTPSKKNGDLDLGYIE
TVCREIGFAIREKSERHTVVVRSTVLPGTVNNVVIPLIEDCSGKKAGVDF
GVGTNPEFLRESTAIKDYDFPPMTVIGELDKQTGDLLEEIYRELDAPIIR
KTVEVAEMIKYTCNVWHAAKVTFANEIGNIAKAVGVDGREVMDVICQDHK
LNLSRYYMRPGFAFGGSCLPKDVRALTYRASQLDVEHPMLGSLMRSNSNQ
VQKAFDLITSHDTRKVGLLGLSFKAGTDDLRESPLVELAEMLIGKGYELR
IFDRNVEYARVHGANKEYIESKIPHVSSLLVSDLDEVVASSDVLVLGNGD
ELFVDLVNKTPSGKKLVDLVGFMPHTTTAQAEGICW
3D structure
PDB1mv8 The crystal structure of GDP-mannose dehydrogenase: A key enzyme in alginate biosynthesis of P. aeruginosa
ChainD
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T124 E161 K210 N214 C268 D272
Catalytic site (residue number reindexed from 1) T124 E161 K210 N214 C268 D272
Enzyme Commision number 1.1.1.132: GDP-mannose 6-dehydrogenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0047919 GDP-mannose 6-dehydrogenase activity
GO:0051287 NAD binding
Biological Process
GO:0006970 response to osmotic stress
GO:0036460 cellular response to cell envelope stress
GO:0042121 alginic acid biosynthetic process
GO:0044010 single-species biofilm formation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1mv8, PDBe:1mv8, PDBj:1mv8
PDBsum1mv8
PubMed12705829
UniProtP11759|ALGD_PSEAE GDP-mannose 6-dehydrogenase (Gene Name=algD)

[Back to BioLiP]