Structure of PDB 4dn1 Chain B

Receptor sequence
>4dn1B (length=388) Species: 176299 (Agrobacterium fabrum str. C58) [Search protein sequence]
MNSPIATVEVFTLTQPRKVPYLGALREGEVVNPNGYIVRKGNRTVYPTFD
RSVLVRMTTEAGTVGWGETYGIVAPGAVAALINDLLAGFVIGRDASDPSA
VYDDLYDMMRVRGYTGGFYVDALAALDIALWDIAGQEAGKSIRDLLGGGV
DSFPAYVSGLPERTLKARGELAKYWQDRGFNAFKFATPVADDGPAAEIAN
LRQVLGPQAKIAADMHWNQTPERALELIAEMQPFDPWFAEAPVWTEDIAG
LEKVSKNTDVPIAVGEEWRTHWDMRARIERCRIAIVQPEMGHKGITNFIR
IGALAAEHGIDVIPHATVGAGIFLAASLQASSTLSMLKGHEFQHSIFEPN
RRLLDGDMDCREGRYHLPSGPGLGVRPSEAALGLIERI
3D structure
PDB4dn1 Crystal structure of an enolase (mandelate racemase subgroup member) from Agrobacterium tumefaciens (target EFI-502088) with bound mg and formate
ChainB
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F180 A182 K184 A186 A212 D214 H216 E240 G265 E266 Q287 P288 E289 H315 T317 E341
Catalytic site (residue number reindexed from 1) F180 A182 K184 A186 A212 D214 H216 E240 G265 E266 Q287 P288 E289 H315 T317 E341
Enzyme Commision number ?
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 MG B D214 E240 E266 D214 E240 E266
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4dn1, PDBe:4dn1, PDBj:4dn1
PDBsum4dn1
PubMed
UniProtA9CL63

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