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3QFK

2.05 Angstrom Crystal Structure of Putative 5'-Nucleotidase from Staphylococcus aureus in complex with alpha-ketoglutarate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008252molecular_functionnucleotidase activity
A0009166biological_processnucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 512
ChainResidue
AASP11
AHIS13
AASP56
AHIS233
AMN513
AHOH623
AHOH720

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 513
ChainResidue
AHIS191
AHIS231
AZN512
AHOH623
AASP56
AASN93

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AKG A 514
ChainResidue
AHIS94
APHE370
AASN372
APHE416
ATYR461
AHOH548
AHOH687
AHOH723

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 515
ChainResidue
AASN82
AASN111
ASER425
AMSE442
AASP506
AHOH602

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 516
ChainResidue
APHE349
AASP350
APRO413
AGLN414
AHIS415
APHE416

Functional Information from PROSITE/UniProt
site_idPS00786
Number of Residues12
Details5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. FdfgtLGNHEFN
ChainResidueDetails
APHE86-ASN97

224201

PDB entries from 2024-08-28

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