Structure of PDB 1mpy Chain D

Receptor sequence
>1mpyD (length=307) Species: 303 (Pseudomonas putida) [Search protein sequence]
MNKGVMRPGHVQLRVLDMSKALEHYVELLGLIEMDRDDQGRVYLKAWTEV
DKFSLVLREADEPGMDFMGFKVVDEDALRQLERDLMAYGCAVEQLPAGEL
NSCGRRVRFQAPSGHHFELYADKEYTGKWGLNDVNPEAWPRDLKGMAAVR
FDHALMYGDELPATYDLFTKVLGFYLAEQVLDENGTRVAQFLSLSTKAHD
VAFIHHPEKGRLHHVSFHLETWEDLLRAADLISMTDTSIDIGPTRHGLTH
GKTIYFFDPSGNRNEVFCGGDYNYPDHKPVTWTTDQLGKAIFYHDRILNE
RFMTVLT
3D structure
PDB1mpy An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2.
ChainD
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H153 H199 H214 H246 Y255 E265
Catalytic site (residue number reindexed from 1) H153 H199 H214 H246 Y255 E265
Enzyme Commision number 1.13.11.2: catechol 2,3-dioxygenase.
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 FE2 D H153 H214 E265 H153 H214 E265
BS02 ACN D F191 H246 F191 H246
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008198 ferrous iron binding
GO:0018577 catechol 2,3-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0042203 toluene catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1mpy, PDBe:1mpy, PDBj:1mpy
PDBsum1mpy
PubMed10368270
UniProtP06622|XYLE1_PSEPU Metapyrocatechase (Gene Name=xylE)

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