Structure of PDB 3dbn Chain B

Receptor sequence
>3dbnB (length=349) Species: 391295 (Streptococcus suis 05ZYH33) [Search protein sequence]
GSHMKMSFRWYGKKDPVTLEEIKAIPGMQGIVTAVYDVPVGQAWPLENIL
ELKKMVEEAGLEITVIESIPVHEDIKQGKPNRDALIENYKTSIRNVGAAG
IPVVCYNFMPVFDWTRSDLHHPLPDGSTSLAFLKSDLAGVDPVAIIENYR
QNISEEDLWANLEYFIKAILPTAEEAGVKMAIHPDDPPYGIFGLPRIITG
QEAVERFLNLYDSEHNGITMCVGSYASDPKNDVLAMTEYALKRNRINFMH
TRNVTAGAWGFQETAHLSQAGDIDMNAVVKLLVDYDWQGSLRPDHGRRIW
GDQTKTPGYGLYDRALGATYFNGLYEANMRAAGKTPDFGIKAKTVGTKE
3D structure
PDB3dbn Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H219 C257 H286 D330 H331 Y345
Catalytic site (residue number reindexed from 1) H183 C221 H250 D294 H295 Y309
Enzyme Commision number 4.2.1.8: mannonate dehydratase.
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 MN B H219 C257 H286 R288 D330 H183 C221 H250 R252 D294
Gene Ontology
Molecular Function
GO:0008198 ferrous iron binding
GO:0008927 mannonate dehydratase activity
GO:0016829 lyase activity
GO:0030145 manganese ion binding
Biological Process
GO:0006064 glucuronate catabolic process
GO:0042840 D-glucuronate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3dbn, PDBe:3dbn, PDBj:3dbn
PDBsum3dbn
PubMed19617363
UniProtA4VVI4|UXUA_STRSY Mannonate dehydratase (Gene Name=uxuA)

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