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

1TV8

Structure of MoaA in complex with S-adenosylmethionine

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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1403
ChainResidue
ATYR30
ASER126
ALEU127
AASP128
APHE135
AHOH1528

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2403
ChainResidue
BASP128
BPHE135
BHOH2506
BCYS28
BSER126
BLEU127

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SAM A 1501
ChainResidue
ATYR30
ATHR73
AGLY75
AGLU76
ATHR102
ATHR103
AASN104
ASER126
AVAL167
APHE196
AMET197
ASF41401
AHOH1570

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAM B 2501
ChainResidue
BTYR30
BTHR73
BGLY75
BGLU76
BTHR102
BTHR103
BASN104
BSER126
BVAL167
BMET197
BSF42401
BHOH2506
BHOH2517
BHOH2525

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 1401
ChainResidue
ACYS24
APHE26
ACYS28
ACYS31
AMET32
AGLY75
AASN104
ASAM1501

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 1402
ChainResidue
ACYS261
ACYS264
ACYS278
ALEU279
ATYR316
ASER317
ADTU1502

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 B 2401
ChainResidue
BCYS24
BPHE26
BCYS28
BCYS31
BMET32
BGLY75
BASN104
BSAM2501

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 2402
ChainResidue
BCYS261
BCYS264
BCYS278
BLEU279
BASP314
BSER317

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DTU A 1502
ChainResidue
ASER255
APHE260
AARG266
ALEU279
ASF41402

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:0000255|HAMAP-Rule:MF_01225
ChainResidueDetails
AARG17
ALYS163
AMET197
ACYS261
ACYS264
AARG266
ACYS278
BARG17
BCYS24
BCYS28
BTYR30
ACYS24
BCYS31
BARG71
BGLY75
BTHR102
BSER126
BLYS163
BMET197
BCYS261
BCYS264
BARG266
ACYS28
BCYS278
ATYR30
ACYS31
AARG71
AGLY75
ATHR102
ASER126

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon