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2FB3

Structure of MoaA in complex with 5'-GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005525molecular_functionGTP binding
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0016829molecular_functionlyase activity
A0019008cellular_componentmolybdopterin synthase complex
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0061798molecular_functionGTP 3',8'-cyclase activity
A0061799molecular_functioncyclic pyranopterin monophosphate synthase activity
A1904047molecular_functionS-adenosyl-L-methionine binding
B0003824molecular_functioncatalytic activity
B0005525molecular_functionGTP binding
B0006777biological_processMo-molybdopterin cofactor biosynthetic process
B0016829molecular_functionlyase activity
B0019008cellular_componentmolybdopterin synthase complex
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0061798molecular_functionGTP 3',8'-cyclase activity
B0061799molecular_functioncyclic pyranopterin monophosphate synthase activity
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ACYS28
ATYR30
ASER126
ALEU127
AASP128
APHE135
AHOH585

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BLEU127
BASP128
BCYS28
BSER126

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MET A 500
ChainResidue
ATHR73
AGLY75
AGLU76
ATHR102
ATHR103
ASER126
ASF4401
A5AD501

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MET B 501
ChainResidue
BGLY75
BGLU76
BTHR102
BTHR103
BASN104
BSER126
BSF4401

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SF4 A 401
ChainResidue
ACYS24
APHE26
ACYS28
ACYS31
AMET500

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 A 402
ChainResidue
ACYS261
ACYS264
ACYS278
ATYR316
ASER317
AGTP404

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GTP A 404
ChainResidue
AARG17
ALYS69
AARG71
ATHR102
AASN124
ALYS163
AASN165
AARG192
APHE260
AARG266
AARG268
ASF4402
A5AD501

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 5AD A 501
ChainResidue
ATYR30
ASER126
AVAL167
AMET197
AGTP404
AMET500
AHOH532
AHOH585

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 401
ChainResidue
BCYS24
BPHE26
BCYS28
BCYS31
BMET32
BGLY75
BASN104
BMET501

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 402
ChainResidue
BCYS261
BCYS264
BCYS278
BASP314
BTYR316
BSER317

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE POP B 404
ChainResidue
BARG71
BASN124
BARG192
BHOH531

Functional Information from PROSITE/UniProt
site_idPS01305
Number of Residues12
DetailsMOAA_NIFB_PQQE moaA / nifB / pqqE family signature. VtdrCNFRCdYC
ChainResidueDetails
AVAL20-CYS31

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:16632608, ECO:0007744|PDB:2FB3
ChainResidueDetails
ACYS28
ATYR30
ACYS31
AARG71
AGLY75
ATHR102
ASER126
ALYS163
AMET197
ACYS261
ACYS264
AARG266
ACYS278
BARG17
BCYS24
BCYS28
BTYR30
BCYS31
BARG71
BGLY75
BTHR102
BSER126
BLYS163
BMET197
BCYS261
BCYS264
BARG266
BCYS278
AARG17
ACYS24

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PDB entries from 2024-06-12

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