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6Z88

human GTP cyclohydrolase I in complex with allosteric inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003934molecular_functionGTP cyclohydrolase I activity
A0046654biological_processtetrahydrofolate biosynthetic process
B0003934molecular_functionGTP cyclohydrolase I activity
B0046654biological_processtetrahydrofolate biosynthetic process
C0003934molecular_functionGTP cyclohydrolase I activity
C0046654biological_processtetrahydrofolate biosynthetic process
D0003934molecular_functionGTP cyclohydrolase I activity
D0046654biological_processtetrahydrofolate biosynthetic process
E0003934molecular_functionGTP cyclohydrolase I activity
E0046654biological_processtetrahydrofolate biosynthetic process
F0003934molecular_functionGTP cyclohydrolase I activity
F0046654biological_processtetrahydrofolate biosynthetic process
G0003934molecular_functionGTP cyclohydrolase I activity
G0046654biological_processtetrahydrofolate biosynthetic process
H0003934molecular_functionGTP cyclohydrolase I activity
H0046654biological_processtetrahydrofolate biosynthetic process
I0003934molecular_functionGTP cyclohydrolase I activity
I0046654biological_processtetrahydrofolate biosynthetic process
J0003934molecular_functionGTP cyclohydrolase I activity
J0046654biological_processtetrahydrofolate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue QBK A 301
ChainResidue
AASP127
AMET129
ALEU157
ATHR240
AGLU243
ESER228
EARG235
EARG241
EHOH313

site_idAC2
Number of Residues9
Detailsbinding site for residue QBK A 302
ChainResidue
ASER228
AMET230
AARG235
AARG241
CASP127
CMET129
CLEU157
CTHR240
CGLU243

site_idAC3
Number of Residues2
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS141
BHIS144

site_idAC4
Number of Residues10
Detailsbinding site for residue QBK B 302
ChainResidue
BSER228
BMET230
BARG235
BARG241
FASP127
FMET129
FLEU157
FTHR240
FGLU243
FHOH403

site_idAC5
Number of Residues11
Detailsbinding site for residue QBK C 301
ChainResidue
CSER228
CMET230
CARG235
CARG241
CHOH403
CHOH406
IASP127
IMET129
ILEU157
ITHR240
IGLU243

site_idAC6
Number of Residues8
Detailsbinding site for residue QBK D 301
ChainResidue
BASP127
BLEU157
BTHR240
BGLU243
DSER228
DMET230
DARG235
DARG241

site_idAC7
Number of Residues8
Detailsbinding site for residue QBK D 302
ChainResidue
DLEU157
DTHR240
DGLU243
DHOH405
HSER228
HMET230
HARG235
HARG241

site_idAC8
Number of Residues8
Detailsbinding site for residue QBK F 302
ChainResidue
FSER228
FMET230
FARG235
FARG241
JASP127
JLEU157
JTHR240
JGLU243

site_idAC9
Number of Residues8
Detailsbinding site for residue QBK G 301
ChainResidue
ELEU157
ETHR240
EGLU243
EHOH302
GSER228
GMET230
GARG235
GARG241

site_idAD1
Number of Residues10
Detailsbinding site for residue QBK G 302
ChainResidue
GASP127
GMET129
GLEU157
GTHR240
GGLU243
GHOH402
ISER228
IMET230
IARG235
IARG241

site_idAD2
Number of Residues8
Detailsbinding site for residue QBK J 301
ChainResidue
HASP127
HLEU157
HTHR240
HGLU243
JSER228
JMET230
JARG235
JARG241

Functional Information from PROSITE/UniProt
site_idPS00859
Number of Residues17
DetailsGTP_CYCLOHYDROL_1_1 GTP cyclohydrolase I signature 1. EMVivKDIdmfSmCEHH
ChainResidueDetails
AGLU128-HIS144

site_idPS00860
Number of Residues11
DetailsGTP_CYCLOHYDROL_1_2 GTP cyclohydrolase I signature 2. SrRlQVQERLT
ChainResidueDetails
ASER176-THR186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11087827","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17704208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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