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1FB1

CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
ACYS141
AHIS144
ACYS212
BIPA302

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BCYS141
BHIS144
BCYS212
BIPA303

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 300
ChainResidue
CHIS144
CCYS212
DIPA304
CCYS141

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 300
ChainResidue
DCYS141
DHIS144
DCYS212
DIPA305

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 300
ChainResidue
AIPA306
ECYS141
EHIS144
ECYS212

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IPA B 302
ChainResidue
AHIS144
AZN300
BGLY164
BLEU165

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA B 303
ChainResidue
BCYS141
BHIS143
BHIS144
BZN300
CLEU165
CSER166

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA D 304
ChainResidue
CHIS143
CHIS144
CZN300
DGLY164
DLEU165
DSER166

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA D 305
ChainResidue
DHIS143
DZN300
ESER166

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IPA A 306
ChainResidue
ALEU165
ASER166
ECYS141
EHIS143
EHIS144
EZN300

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 Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:11087827
ChainResidueDetails
ACYS141
DCYS141
DHIS144
DCYS212
ECYS141
EHIS144
ECYS212
AHIS144
ACYS212
BCYS141
BHIS144
BCYS212
CCYS141
CHIS144
CCYS212

site_idSWS_FT_FI2
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER60
BSER60
CSER60
DSER60
ESER60

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17704208
ChainResidueDetails
ASER81
BSER81
CSER81
DSER81
ESER81

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gtp
ChainResidueDetails
AHIS143
AHIS210

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gtp
ChainResidueDetails
BHIS143
BHIS210

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gtp
ChainResidueDetails
CHIS143
CHIS210

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gtp
ChainResidueDetails
DHIS143
DHIS210

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1gtp
ChainResidueDetails
EHIS143
EHIS210

224572

PDB entries from 2024-09-04

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