Structure of PDB 4aq2 Chain L

Receptor sequence

>4aq2L (length=419) Species: 160488 (Pseudomonas putida KT2440)

LHYLSGFGNEFASEALPGALPVGQNSPQKAPYGLYAELLSGTAFTMARSE
LRRTWLYRIRPSALHPRFERLARQPLGGPLGGINPNRLRWSPQPIPAEPT
DFIEGWLPMAANAGAEKPAGVSIYIYRANRSMERVFFNADGELLLVPEQG
RLRIATELGVMEVEPLEIAVIPRGMKFRVELLDGQARGYIAENHGAPLRL
PDLGPIGSNGLANPRDFLTPVAHYEEAEGPVQLVQKFLGEHWACELQHSP
LDVVAWHGSNVPYKYDLRRFNTIGTVSFDHPDPSIFTVLTSPTSVHGMAN
MDFVIFPPRWMVAENTFRPPWFHRNLMNEFMGLINGAGFLPGGASLHGVM
SAHGPDAETCEKAIAADLAPHKIDNTMAFMFETSQVLRPSLQALECPQLQ
ADYDSCWATLPSTFNPNRR

3D structure

• PDB: 4aq2 Visualizing the Substrate-, Superoxo-, Alkylperoxo-, and Product-Bound States at the Nonheme Fe(II) Site of Homogentisate Dioxygenase.
• Chain: L
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H288 H331 E337 H361 H367
• Catalytic site (residue number reindexed from 1): H280 H323 E329 H347 H353
• Enzyme Commision number: 1.13.11.5: homogentisate 1,2-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	L	H331 E337 H367	H323 E329 H353

Gene Ontology

Molecular Function

• GO:0000976 transcription cis-regulatory region binding
• GO:0001217 DNA-binding transcription repressor activity
• GO:0004411 homogentisate 1,2-dioxygenase activity
• GO:0005506 iron ion binding
• GO:0046872 metal ion binding
• GO:0051213 dioxygenase activity

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0006559 L-phenylalanine catabolic process
• GO:0006570 tyrosine metabolic process
• GO:0006572 tyrosine catabolic process
• GO:0045892 negative regulation of DNA-templated transcription

Cellular Component

• GO:0005737 cytoplasm
• GO:0032993 protein-DNA complex

External links

• PDB: RCSB:4aq2, PDBe:4aq2, PDBj:4aq2
• PDBsum: 4aq2
• PubMed: 23858455
• UniProt: Q88E47|HGD_PSEPK Homogentisate 1,2-dioxygenase (Gene Name=hmgA)