Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2FB2

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

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
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 Residues30
DetailsBINDING: BINDING => ECO:0000269|PubMed:16632608, ECO:0007744|PDB:2FB3
ChainResidueDetails
ACYS28
ATYR30
ACYS31
AARG71
AGLY75
ATHR102
ASER126
ALYS163
AMET197
ACYS261
ACYS264
AALA266
ACYS278
BALA17
BCYS24
BCYS28
BTYR30
BCYS31
BARG71
BGLY75
BTHR102
BSER126
BLYS163
BMET197
BCYS261
BCYS264
BALA266
BCYS278
AALA17
ACYS24

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon