Structure of PDB 1mfz Chain A

Receptor sequence
>1mfzA (length=436) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
MRISIFGLGYVGAVCAGCLSARGHEVIGVDVSSTKIDLINQGKSPIVEPG
LEALLQQGRQTGRLSGTTDFKKAVLDSDVSFICVGTPSKKNGDLDLGYIE
TVCREIGFAIREKSERHTVVVRSTVLPGTVNNVVIPLIEDCSGKKAGVDF
GVGTNPEFLRESTAIKDYDFPPMTVIGELDKQTGDLLEEIYRELDAPIIR
KTVEVAEMIKYTCNVWHAAKVTFANEIGNIAKAVGVDGREVMDVICQDHK
LNLSRYYMRPGFAFGGSCLPKDVRALTYRASQLDVEHPMLGSLMRSNSNQ
VQKAFDLITSHDTRKVGLLGLSFKAGTDDLRESPLVELAEMLIGKGYELR
IFDRNVEYARVHGANKEYIESKIPHVSSLLVSDLDEVVASSDVLVLGNGD
ELFVDLVNKTPSGKKLVDLVGFMPHTTTAQAEGICW
3D structure
PDB1mfz The crystal structure of GDP-mannose dehydrogenase: A key enzyme in alginate biosynthesis of P. aeruginosa
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GDX A F158 L159 R160 E161 K210 N214 V221 F158 L159 R160 E161 K210 N214 V221
BS02 GDX A Y256 Y257 R259 F264 G265 C268 L269 F323 K324 Y256 Y257 R259 F264 G265 C268 L269 F323 K324
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1mfz, PDBe:1mfz, PDBj:1mfz
PDBsum1mfz
PubMed12705829
UniProtP11759|ALGD_PSEAE GDP-mannose 6-dehydrogenase (Gene Name=algD)

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