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2BZ0

Crystal Structure of E. coli GTP cyclohydrolase II in complex with GTP analogue, GMPcPP, and Zinc

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
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
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003935molecular_functionGTP cyclohydrolase II activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0009231biological_processriboflavin biosynthetic process
B0016787molecular_functionhydrolase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A1174
ChainResidue
ACYS54
ACYS65
ACYS67

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A1175
ChainResidue
AHIS51
ASER52
AG2P1176

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B1174
ChainResidue
BG2P1175
BCYS54
BCYS65
BCYS67

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE G2P A1176
ChainResidue
AARG49
ASER52
AGLU53
ACYS54
AGLN70
AGLN91
AGLU92
AGLY93
AARG94
ALYS101
AGLN108
ATHR114
AARG128
ATHR149
AASN151
ALYS154
AMG1175
AHOH2044
AHOH2059

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE G2P B1175
ChainResidue
BARG49
BSER52
BGLU53
BCYS54
BGLN70
BGLN91
BGLU92
BGLY93
BARG94
BLYS101
BTYR105
BGLN108
BTHR114
BASN118
BARG128
BTHR149
BASN151
BLYS154
BZN1174
BHOH2033
BHOH2034

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255
ChainResidueDetails
AASP126
BASP126

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AARG128
BARG128

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AARG49
BARG49
BCYS54
BCYS65
BCYS67
BGLN70
BGLU92
BTHR114
BTHR149
BLYS154
ACYS54
ACYS65
ACYS67
AGLN70
AGLU92
ATHR114
ATHR149
ALYS154

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PDB entries from 2024-11-13

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