Structure of PDB 1ey2 Chain A

Receptor sequence

>1ey2A (length=419) Species: 9606 (Homo sapiens)

AELKYISGFGNECSSEDPRCPGSLPEGQNNPQVCPYNLYAEQLSGSAFTC
PRSTNKRSWLYRILPSVSHKPFESIDEGHVTHNWDEVDPDPNQLRWKPFE
IPKASQKKVDFVSGLHTLCGAGDIKSNNGLAIHIFLCNTSMENRCFYNSD
GDFLIVPQKGNLLIYTEFGKMLVQPNEICVIQRGMRFSIDVFEETRGYIL
EVYGVHFELPDLGPIGANGLANPRDFLIPIAWYEDRQVPGGYTVINKYQG
KLFAAKQDVSPFNVVAWHGNYTPYKYNLKNFMVINSVAFDHADPSIFTVL
TAKSVRPGVAIADFVIFPPRWGVADKTFRPPYYHRNCMSEFMGLIRGFLP
GGGSLHSTMTPHGPDADCFEKASKVKLAPERIADGTMAFMFESSLSLAVT
KWGLKASRLKSHFTPNSRN

3D structure

• PDB: 1ey2 Crystal structure of human homogentisate dioxygenase.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H292 H335 E341 H365 H371
• Catalytic site (residue number reindexed from 1): H291 H334 E340 H356 H362
• 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	FE2	A	H335 E341 H371	H334 E340 H362

Gene Ontology

Molecular Function

• GO:0004411 homogentisate 1,2-dioxygenase activity
• GO:0005515 protein binding
• GO:0042802 identical protein 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

Cellular Component

• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:1ey2, PDBe:1ey2, PDBj:1ey2
• PDBsum: 1ey2
• PubMed: 10876237
• UniProt: Q93099|HGD_HUMAN Homogentisate 1,2-dioxygenase (Gene Name=HGD)