Structure of PDB 2pcd Chain M

Receptor sequence
>2pcdM (length=233) Species: 303 (Pseudomonas putida) [Search protein sequence]
PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPN
FSHLGFGAHDHDLLLNFGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQAN
AGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGP
NDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQ
LIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFE
3D structure
PDB2pcd Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution.
ChainM
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 M Y408 Y447 H460 H462 Y105 Y144 H157 H159
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:2pcd, PDBe:2pcd, PDBj:2pcd
PDBsum2pcd
PubMed7990141
UniProtP00437|PCXB_PSEPU Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)

[Back to BioLiP]