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5TPG

Optimization of spirocyclic proline tryptophanhydroxylase-1 inhibitors

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 Residues4
Detailsbinding site for residue FE A 501
ChainResidue
AHIS272
AHIS277
AGLU317
ATRS502

site_idAC2
Number of Residues12
Detailsbinding site for residue TRS A 502
ChainResidue
AGLU273
AHIS277
ATYR312
AGLU317
AFE501
A7H5505
AHOH645
ATYR235
APHE241
APHE250
APRO268
AHIS272

site_idAC3
Number of Residues5
Detailsbinding site for residue CCN A 503
ChainResidue
AILE171
AASN210
AILE211
AGLN213
AHOH715

site_idAC4
Number of Residues7
Detailsbinding site for residue CCN A 504
ChainResidue
AGLU292
AMET386
AARG387
ATHR390
AHOH655
AHOH699
AHOH765

site_idAC5
Number of Residues22
Detailsbinding site for residue 7H5 A 505
ChainResidue
ATYR235
ALEU236
APRO238
APHE241
ALEU242
AARG257
ATYR264
ATHR265
APRO266
AGLU267
APRO268
AHIS272
AALA309
ATYR312
AGLU317
ASER336
ASER337
ACYS364
AILE366
ATRS502
AHOH637
AHOH724

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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