Structure of PDB 3i4k Chain B

Receptor sequence
>3i4kB (length=370) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
DLTIQKVESRILDVPLIRPHGFATTTSTEQHILLVSVHLENGVIGYGEGV
VPGGPWWGGESVETMKALVDGYLAPVLIGRAVSELAGIMADLERVVARAR
YAKAAVDVAMHDAWARSLNVPVRDLLGGTVRDKVDVTWALGVLPLDVAVA
EIEERIEEFGNRSFKLKMGAGDPAEDTRRVAELAREVGDRVSLRIDINAR
WDRRTALHYLPILAEAGVELFEQPTPADDLETLREITRRTNVSVMADESV
WTPAEALAVVKAQAADVIALKTTKHGGLLESKKIAAIAEAGGLACHGATS
LEGPIGTAASLQFAASTKAISYGTELFGPQLLKDTYIVQEFEYKDGQVAI
PQGPGLGVDVDMDKVNFYTR
3D structure
PDB3i4k Crystal structure of Muconate lactonizing enzyme from Corynebacterium glutamicum
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H24 V55 G58 G91 A143 K169 K171 D200 N202 E226 D251 E252 S253 A273 K275 T276 A302 T303 S304 T328 E329 L330
Catalytic site (residue number reindexed from 1) H20 V51 G54 G87 A139 K165 K167 D196 N198 E222 D247 E248 S249 A269 K271 T272 A298 T299 S300 T324 E325 L326
Enzyme Commision number 5.5.1.1: muconate cycloisomerase.
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 D200 E226 D251 D196 E222 D247
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0018849 muconate cycloisomerase activity
GO:0018850 chloromuconate cycloisomerase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3i4k, PDBe:3i4k, PDBj:3i4k
PDBsum3i4k
PubMed
UniProtQ8NN12

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