Structure of PDB 3pcm Chain R

Receptor sequence
>3pcmR (length=233) Species: 303 (Pseudomonas putida) [Search protein sequence]
PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPN
FSHLGFGAHDHDLLLNFGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQAN
AGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGP
NDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQ
LIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFE
3D structure
PDB3pcm Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding.
ChainR
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y408 Y447 R457 H460 H462
Catalytic site (residue number reindexed from 1) Y105 Y144 R154 H157 H159
Enzyme Commision number 1.13.11.3: protocatechuate 3,4-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 FE R Y408 H460 H462 Y105 H157 H159
BS02 NNO R Y324 W449 R457 H460 H462 I491 Y24 W146 R154 H157 H159 I188
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005506 iron ion binding
GO:0008199 ferric iron binding
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0018578 protocatechuate 3,4-dioxygenase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0019619 3,4-dihydroxybenzoate catabolic process
GO:0042952 beta-ketoadipate pathway

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3pcm, PDBe:3pcm, PDBj:3pcm
PDBsum3pcm
PubMed9254600
UniProtP00437|PCXB_PSEPU Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)

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