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4RL4

Crystal structure of GTP cyclohydrolase II from Helicobacter pylori 26695

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003935molecular_functionGTP cyclohydrolase II activity
A0005525molecular_functionGTP binding
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0009231biological_processriboflavin biosynthetic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003935molecular_functionGTP cyclohydrolase II activity
B0005525molecular_functionGTP binding
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009231biological_processriboflavin biosynthetic process
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PPV A 201
ChainResidue
AARG50
AARG128
ATHR149
AASN150
AASN151
ALYS154
AHOH327

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PPV B 201
ChainResidue
BTHR149
BASN150
BASN151
BLYS154
BLEU169
BHOH333
BARG50
BARG128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00179","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00179","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00179","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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