Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5L01

Tryptophan 5-hydroxylase in complex with inhibitor (3~{S})-8-[2-azanyl-6-[(1~{R})-1-(4-chloranyl-2-phenyl-phenyl)-2,2,2-tris(fluoranyl)ethoxy]pyrimidin-4-yl]-2,8-diazaspiro[4.5]decane-3-carboxylic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0002576biological_processplatelet degranulation
A0004497molecular_functionmonooxygenase activity
A0004510molecular_functiontryptophan 5-monooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007623biological_processcircadian rhythm
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
A0030279biological_processnegative regulation of ossification
A0035902biological_processresponse to immobilization stress
A0042427biological_processserotonin biosynthetic process
A0043005cellular_componentneuron projection
A0045600biological_processpositive regulation of fat cell differentiation
A0046849biological_processbone remodeling
A0046872molecular_functionmetal ion binding
A0060749biological_processmammary gland alveolus development
A1900046biological_processregulation of hemostasis
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE A 501
ChainResidue
AHIS272
AHIS277
AGLU317
AHOH627
AHOH655

site_idAC2
Number of Residues18
Detailsbinding site for residue 6Z4 A 502
ChainResidue
APRO266
AGLU267
APRO268
AHIS272
AALA309
APHE313
AGLU317
AGLY333
ASER336
ASER337
ACYS364
AILE366
AHOH629
AHOH655
ALEU236
AARG257
ATYR264
ATHR265

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
ASER336
AILE366
ATYR235
AARG257
ATHR265

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

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
ASER58

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon