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1MLW

Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)

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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 403
ChainResidue
AHIS272
AHIS277
AGLU317
AHOH600
AHOH601
AHOH602
AHBI900

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HBI A 900
ChainResidue
ATYR235
ALEU236
APRO238
APHE241
ATYR312
AFE403
AHOH506
AHOH600
AHOH601
AHOH629
AHOH682
AHOH719
AVAL232
AGLY234

Functional Information from PROSITE/UniProt
site_idPS00367
Number of Residues12
DetailsBH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDtcHELLGHVP
ChainResidueDetails
APRO268-PRO279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P70080
ChainResidueDetails
ATYR235
AARG257
ATHR265
ASER336
AILE366

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12379098, ECO:0007744|PDB:1MLW
ChainResidueDetails
AHIS272
AHIS277
AGLU317

222036

PDB entries from 2024-07-03

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