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2FB3

Structure of MoaA in complex with 5'-GTP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005525molecular_functionGTP binding
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0016829molecular_functionlyase activity
A0032324biological_processmolybdopterin cofactor biosynthetic process
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
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0005525molecular_functionGTP binding
B0006777biological_processMo-molybdopterin cofactor biosynthetic process
B0016829molecular_functionlyase activity
B0032324biological_processmolybdopterin cofactor biosynthetic process
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 Residues438
DetailsDomain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16632608","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2FB3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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