Structure of PDB 3fcp Chain H

Receptor sequence
>3fcpH (length=356) Species: 272620 (Klebsiella pneumoniae subsp. pneumoniae MGH 78578) [Search protein sequence]
LTATVEQIESWIVDVPTICQSLVIVRLTRSDGICGIGEATTIGGLSYGVE
SPEAISSAITHYLTPLLKGQPADNLNALTARMNGAIKGNTFAKSAIETAL
LDAQGKALGLPVSALLGGALQTALPVLWTLASGDTAKDIAEGEKLLARAF
KLKIGARELATDLRHTRAIVEALGDRASIRVDVNQAWDAATGAKGCRELA
AMGVDLIEQPVSAHDNAALVRLSQQIETAILADEAVATAYDGYQLAQQGF
TGAYALKIAKAGGPNSVLALARVAQAAGIGLYGGTMLEGTVGTVASLHAW
STLPLQWGTEMFGPLLLKDDIVSVPLTFADGQVALPQTPGLGVELDEDKL
HFYTRQ
3D structure
PDB3fcp Crystal structure of Muconate lactonizing enzyme from Klebsiella pneumoniae
ChainH
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T54 G57 T142 K168 K170 D199 N201 E225 D250 E251 A252 K274 G301 T302 M303 T326 E327 M328
Catalytic site (residue number reindexed from 1) T41 G44 T129 K151 K153 D182 N184 E208 D233 E234 A235 K257 G284 T285 M286 T309 E310 M311
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 H N201 D250 E251 N184 D233 E234
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3fcp, PDBe:3fcp, PDBj:3fcp
PDBsum3fcp
PubMed
UniProtA6T9N5

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