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2BZ1

CRYSTAL STRUCTURE OF APO E. COLI GTP CYCLOHYDROLASE II

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003935molecular_functionGTP cyclohydrolase II activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009231biological_processriboflavin biosynthetic process
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1174
ChainResidue
ACYS54
ACYS65
ACYS67
AHOH2191

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1175
ChainResidue
AHOH2192
AHOH2193
AHOH2194
AARG94
ATYR105
AGLN108
AHOH2137
AHOH2191

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1176
ChainResidue
AARG128
ALYS154
ATAU1179
AHOH2081
AHOH2195

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1177
ChainResidue
APRO152
AARG168
AHOH2198

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TAU A1179
ChainResidue
AARG49
AGLN70
ATHR149
AASN150
ALYS154
ASO41176
AHOH2079
AHOH2203

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A1178
ChainResidue
AGLY57
AASP58
AALA59
ALEU60
APHE61
AHOH2090
AHOH2105
AHOH2199
AHOH2200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues13
DetailsBinding site: {}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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