Structure of PDB 4mmw Chain B Binding Site BS03

Receptor Information
>4mmw Chain B (length=381) Species: 176299 (Agrobacterium fabrum str. C58) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIITDVEVRVFRTTTRRHSDSAGHAHPGPAHQVEQAMLTVRTEDGQEGHS
FTAPEIVRPHVIEKFVKKVLIGEDHRDRERLWQDLAHWQRGSAAQLTDRT
LAVVDCALWDLAGRSLGQPVYKLIGGYRDKVLAYGSIMCGDELEGGLATP
EDYGRFAETLVKRGYKGIKLHTWMPPVSWAPDVKMDLKACAAVREAVGPD
IRLMIDAFHWYSRTDALALGRGLEKLGFDWIEEPMDEQSLSSYKWLSDNL
DIPVVGPESAAGKHWHRAEWIKAGACDILRTGVNDVGGITPALKTMHLAE
AFGMECEVHGNTAMNLHVVAATKNCRWYERGLLHPFLEYDDGHDYLKSLS
DPMDRDGFVHVPDRPGLGEDIDFTFIDNNRV
Ligand information
Ligand IDXYH
InChIInChI=1S/C5H9NO7/c7-1(3(9)5(11)12)2(8)4(10)6-13/h1-3,7-9,13H,(H,6,10)(H,11,12)/p-1/t1-,2-,3+/m0/s1
InChIKeyDMGBHBFPSRKPBV-XZIMBLGRSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NO)C(O)C(O)C(O)C([O-])=O
OpenEye OEToolkits 1.5.0[C@H]([C@@H](C(=O)NO)O)([C@H](C(=O)[O-])O)O
CACTVS 3.341ONC(=O)[CH](O)[CH](O)[CH](O)C([O-])=O
OpenEye OEToolkits 1.5.0C(C(C(=O)NO)O)(C(C(=O)[O-])O)O
CACTVS 3.341ONC(=O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O
FormulaC5 H8 N O7
NameXYLAROHYDROXAMATE
ChEMBL
DrugBankDB03734
ZINC
PDB chain4mmw Chain B Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4mmw Crystal structure of D-glucarate dehydratase from Agrobacterium tumefaciens complexed with magnesium, L-Xylarohydroxamate and L-Lyxarohydroxamate
Resolution1.647 Å
Binding residue
(original residue number in PDB)		H24 C139 K169 H171 D206 H209 E258 H309 E329
Binding residue
(residue number reindexed from 1)		H24 C139 K169 H171 D206 H209 E258 H309 E329
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S136 K169 H171 P181 D206 F208 E232 P257 E258 R280 G282 H309 G310 N311 E329 G331 E338
Catalytic site (residue number reindexed from 1) S136 K169 H171 P181 D206 F208 E232 P257 E258 R280 G282 H309 G310 N311 E329 G331 E338
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0016052 carbohydrate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4mmw, PDBe:4mmw, PDBj:4mmw
PDBsum4mmw
PubMed
UniProtQ7CSI0

[Back to BioLiP]