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2FB2

Structure of the MoaA Arg17/266/268/Ala triple mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005525molecular_functionGTP binding
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0016829molecular_functionlyase activity
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
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
AHOH510

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BLEU127
BASP128
BPHE135
BTYR30
BSER126

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SAM A 501
ChainResidue
ATYR30
ATHR73
AGLY75
AGLU76
ATHR102
ATHR103
ASER126
AVAL167
APHE196
AMET197
ASF4401
AHOH615

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SAM B 501
ChainResidue
BTYR30
BTHR73
BGLY75
BGLU76
BTHR102
BTHR103
BASN104
BSER126
BVAL167
BMET197
BSF4401
BHOH510

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 401
ChainResidue
ACYS24
APHE26
ACYS28
ACYS31
AMET32
AASN104
ASAM501

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SF4 A 402
ChainResidue
ACYS261
ACYS264
ACYS278
ALEU279
ASER317

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 401
ChainResidue
BCYS24
BCYS28
BCYS31
BMET32
BASN104
BSAM501

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SF4 B 402
ChainResidue
BCYS261
BCYS264
BCYS278
BSER317

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

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PDB entries from 2025-08-13

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