Structure of PDB 1nu5 Chain A

Receptor sequence
>1nu5A (length=369) Species: 65067 (Pseudomonas sp. P51) [Search protein sequence]
MKIEAISTTIVDVPTRRPLQMSFTTVHKQSYVIVQVKAGGLVGIGEGGSV
GGPTWGSESAETIKVIIDNYLAPLLVGKDASNLSQARVLMDRAVTGNLSA
KAAIDIALHDLKARALNLSIADLIGGTMRTSIPIAWTLASGDTARDIDSA
LEMIETRRHNRFKVKLGARTPAQDLEHIRSIVKAVGDRASVRVDVNQGWD
EQTASIWIPRLEEAGVELVEQPVPRANFGALRRLTEQNGVAILADESLSS
LSSAFELARDHAVDAFSLKLCNMGGIANTLKVAAVAEAAGISSYGGTMLD
STVGTAAALHVYATLPSLPYGCELIGPWVLGDRLTQQDLEIKDFEVHLPL
GSGLGVDLDHDKVRHYTRA
3D structure
PDB1nu5 The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L19 S49 G52 T137 K163 K165 E176 D194 N196 E220 D245 E246 S247 K269 G296 T297 M298 C322 E323 L324
Catalytic site (residue number reindexed from 1) L19 S49 G52 T137 K163 K165 E176 D194 N196 E220 D245 E246 S247 K269 G296 T297 M298 C322 E323 L324
Enzyme Commision number 5.5.1.7: chloromuconate 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 A D194 E220 D245 D194 E220 D245
BS02 MN A T235 N238 T235 N238
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:0046300 2,4-dichlorophenoxyacetic acid catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1nu5, PDBe:1nu5, PDBj:1nu5
PDBsum1nu5
PubMed12930985
UniProtP27099|TCBD_PSESQ Chloromuconate cycloisomerase (Gene Name=tcbD)

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