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4RL4

Crystal structure of GTP cyclohydrolase II from Helicobacter pylori 26695

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00179
ChainResidueDetails
AASP126
BASP126

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00179
ChainResidueDetails
AARG128
BARG128

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00179
ChainResidueDetails
AARG50
BCYS55
BCYS66
BCYS68
BGLU92
BTHR114
BTHR149
BLYS154
ACYS55
ACYS66
ACYS68
AGLU92
ATHR114
ATHR149
ALYS154
BARG50

222624

PDB entries from 2024-07-17

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