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

1G8R

MOEA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0016740molecular_functiontransferase activity
A0032324biological_processmolybdopterin cofactor biosynthetic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0061599molecular_functionmolybdopterin molybdotransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006777biological_processMo-molybdopterin cofactor biosynthetic process
B0016740molecular_functiontransferase activity
B0032324biological_processmolybdopterin cofactor biosynthetic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0061599molecular_functionmolybdopterin molybdotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 412
ChainResidue
BASP203
BTHR204
BASN205
BSER250
BGLY251
BGLY299
BHOH467

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 413
ChainResidue
BLYS177
BVAL178
BLEU216
BGLY217
BSER320
BGOL418
BHOH515
BGLY37
BARG176

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 414
ChainResidue
AHOH465
BSER378
BLEU379
BGLY380

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 412
ChainResidue
AASP241
AALA244
AASP245
AASN291

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 413
ChainResidue
ASER378
ALEU379
AGLY380
AHOH494
AHOH506
BHOH425

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 414
ChainResidue
ALYS279
APRO280
AGLY281
AARG345
ASER371
AHOH420
AHOH447

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 415
ChainResidue
BASP241
BGLN243
BALA244
BASP245
BASN291

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 415
ChainResidue
AILE201
AASP203
ATHR204
AASN205
AGLY251
AGLY299
AHOH427

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 416
ChainResidue
AGLY409
BARG155
BASN405
BALA406
BHOH447

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 417
ChainResidue
BGLY186
BGLU188
BASP228
BGLY252
BASP259
BHOH495

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 418
ChainResidue
BARG155
BLEU216
BSER320
BASN322
BGOL413
BHOH485

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 419
ChainResidue
BASP11
BLEU14
BASN15

Functional Information from PROSITE/UniProt
site_idPS01079
Number of Residues34
DetailsMOCF_BIOSYNTHESIS_2 Molybdenum cofactor biosynthesis proteins signature 2. SvGeaDytktiLeelgeiafwk..LaiKPGKPfaFG
ChainResidueDetails
ASER254-GLY287

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon