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4V06

Crystal structure of human tryptophan hydroxylase 2 (TPH2), catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0009072biological_processaromatic amino acid metabolic process
A0016714molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0009072biological_processaromatic amino acid metabolic process
B0016714molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD A 600
ChainResidue
APHE296
AHIS318
AGLU319
AHIS323
AGLU363
AFE1491
AHOH2054

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD B 600
ChainResidue
BGLU319
BHIS323
BGLU363
BFE1491
BHOH2013
BPRO314
BHIS318

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 1491
ChainResidue
AHIS318
AHIS323
AGLU363
AIMD600

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 1491
ChainResidue
BHIS318
BHIS323
BGLU363
BIMD600

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDtcHELLGHVP
ChainResidueDetails
APRO314-PRO325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS318
AHIS323
AGLU363
BHIS318
BHIS323
BGLU363

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PDB entries from 2024-07-24

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