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1DI7

1.60 ANGSTROM CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006777biological_processMo-molybdopterin cofactor biosynthetic process
A0016740molecular_functiontransferase activity
A0032324biological_processmolybdopterin cofactor biosynthetic process
A0042802molecular_functionidentical protein binding
A0061598molecular_functionmolybdopterin adenylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AGLY74
AGLY75
ATHR76
AGLY77
AGLY134
AHOH594
AHOH622
AHOH625
AHOH658

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AALA2
AGLU41
ALEU42
APRO172
ATYR173
AARG191
AHOH562
AHOH584
AHOH589

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ATHR3
ATHR3
ATHR3
AHOH559
AHOH559
AHOH559

Functional Information from PROSITE/UniProt
site_idPS01078
Number of Residues14
DetailsMOCF_BIOSYNTHESIS_1 Molybdenum cofactor biosynthesis proteins signature 1. LVLTTGGTGparrD
ChainResidueDetails
ALEU69-ASP82

218853

PDB entries from 2024-04-24

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