Structure of PDB 1muc Chain B

Receptor sequence
>1mucB (length=360) Species: 303 (Pseudomonas putida) [Search protein sequence]
ALIERIDAIIVDLPTIRQQQTLVVLRVRCSDGVEGIGEATTIGGLAYGYE
SPEGIKANIDAHLAPALIGLAADNINAAMLKLDKLAKGNTFAKSGIESAL
LDAQGKRLGLPVSELLGGRVRDSLEVAWTLASGDTARDIAEARHMLEIRR
HRVFKLKIGANPVEQDLKHVVTIKRELGDSASVRVDVNQYWDESQAIRAC
QVLGDNGIDLIEQPISRINRGGQVRLNQRTPAPIMADESIESVEDAFSLA
ADGAASIFALKIAKNGGPRAVLRTAQIAEAAGIGLYGGTMLEGSIGTLAS
AHAFLTLRQLTWGTELFGPLLLTEEIVNEPPQYRDFQLHIPRTPGLGLTL
DEQRLARFAR
3D structure
PDB1muc The refined X-ray structure of muconate lactonizing enzyme from Pseudomonas putida PRS2000 at 1.85 A resolution.
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T53 G56 T141 K167 K169 D198 N200 E224 D249 E250 S251 K273 G300 T301 M302 T326 E327 L328
Catalytic site (residue number reindexed from 1) T41 G44 T129 K155 K157 D186 N188 E212 D237 E238 S239 K261 G288 T289 M290 T314 E315 L316
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 MN B D198 E224 D249 D186 E212 D237
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
GO:0009063 amino acid catabolic process
GO:0042952 beta-ketoadipate pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:1muc, PDBe:1muc, PDBj:1muc
PDBsum1muc
PubMed7500361
UniProtP08310|CATB_PSEPU Muconate cycloisomerase 1 (Gene Name=catB)

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