Structure of PDB 3dbn Chain A

Receptor sequence
>3dbnA (length=349) Species: 391295 (Streptococcus suis 05ZYH33) [Search protein sequence]
SHMKMSFRWYGKKDPVTLEEIKAIPGMQGIVTAVYDVPVGQAWPLENILE
LKKMVEEAGLEITVIESIPVHEDIKQGKPNRDALIENYKTSIRNVGAAGI
PVVCYNFMPVFDWTRSDLHHPLPDGSTSLAFLKSDLAGVDPSKEEMKAII
ENYRQNISEEDLWANLEYFIKAILPTAEEAGVKMAIHPDDPPYGIFGLPR
IITGQEAVERFLNLYDSEHNGITMCVGSYASDPKNDVLAMTEYALKRNRI
NFMHTRNVTAGAWGFQETAHLSQAGDIDMNAVVKLLVDYDWQGSLRPDHG
RRIWGDQTKTPGYGLYDRALGATYFNGLYEANMRAAGKTPDFGIKAKTV
3D structure
PDB3dbn Crystal structures of Streptococcus suis mannonate dehydratase (ManD) and its complex with substrate: genetic and biochemical evidence for a catalytic mechanism
ChainA
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) H187 C225 H254 D298 H299 Y313
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 A H219 C257 H286 D330 H187 C225 H254 D298
BS02 CS2 A R26 W131 H219 D330 H331 P343 Y345 R8 W113 H187 D298 H299 P311 Y313
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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