Structure of PDB 3lxv Chain O

Receptor sequence
>3lxvO (length=238) Species: 303 (Pseudomonas putida) [Search protein sequence]
PAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPN
FSHLGFGAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMW
QANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWR
NGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEA
VQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC
3D structure
PDB3lxv Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis
ChainO
Resolution1.9 Å
3D
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
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 4NC O P487 K493 V501 Q502 I505 P187 K193 V201 Q202 I205
BS02 FE O Y408 H460 H462 Y108 H160 H162
BS03 4NC O Y324 Y408 W449 R457 H460 H462 I491 Y24 Y108 W149 R157 H160 H162 I191
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:3lxv, PDBe:3lxv, PDBj:3lxv
PDBsum3lxv
PubMed
UniProtP00437|PCXB_PSEPU Protocatechuate 3,4-dioxygenase beta chain (Gene Name=pcaH)

[Back to BioLiP]