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4XER

Crystal Structure of C2 form of E112A/H234A Mutant of Stationary Phase Survival Protein (SurE) from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004309molecular_functionexopolyphosphatase activity
A0005737cellular_componentcytoplasm
A0008252molecular_functionnucleotidase activity
A0008253molecular_function5'-nucleotidase activity
A0008254molecular_function3'-nucleotidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0106411molecular_functionXMP 5'-nucleosidase activity
B0000166molecular_functionnucleotide binding
B0004309molecular_functionexopolyphosphatase activity
B0005737cellular_componentcytoplasm
B0008252molecular_functionnucleotidase activity
B0008253molecular_function5'-nucleotidase activity
B0008254molecular_function3'-nucleotidase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0106411molecular_functionXMP 5'-nucleosidase activity
C0000166molecular_functionnucleotide binding
C0004309molecular_functionexopolyphosphatase activity
C0005737cellular_componentcytoplasm
C0008252molecular_functionnucleotidase activity
C0008253molecular_function5'-nucleotidase activity
C0008254molecular_function3'-nucleotidase activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0106411molecular_functionXMP 5'-nucleosidase activity
D0000166molecular_functionnucleotide binding
D0004309molecular_functionexopolyphosphatase activity
D0005737cellular_componentcytoplasm
D0008252molecular_functionnucleotidase activity
D0008253molecular_function5'-nucleotidase activity
D0008254molecular_function3'-nucleotidase activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
D0106411molecular_functionXMP 5'-nucleosidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue ACT A 301
ChainResidue
AALA182
AGLY200
AHOH685

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 302
ChainResidue
AASP8
AASP9
ASER39
AASN92
AHOH482
AHOH483

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 B 301
ChainResidue
BPRO95
BASN96
BASP100
BHOH457
BHOH533
BHOH617

site_idAC4
Number of Residues5
Detailsbinding site for residue MPD B 302
ChainResidue
BALA182
BGLY200
BPRO202
BHOH554
BHOH640

site_idAC5
Number of Residues6
Detailsbinding site for residue MG B 303
ChainResidue
BASP8
BASP9
BASN92
BHOH451
BHOH456
BHOH457

site_idAC6
Number of Residues3
Detailsbinding site for residue PO4 C 301
ChainResidue
CASN96
CASP100
CHOH581

site_idAC7
Number of Residues6
Detailsbinding site for residue MG C 302
ChainResidue
CASP8
CASP9
CASN92
CHOH419
CHOH423
CHOH555

site_idAC8
Number of Residues5
Detailsbinding site for residue MG D 301
ChainResidue
DASP8
DASP9
DSER39
DASN92
DHOH523

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00060
ChainResidueDetails
AASP8
AASP9
ASER39
AASN92
BASP8
BASP9
BSER39
BASN92
CASP8
CASP9
CSER39
CASN92
DASP8
DASP9
DSER39
DASN92

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PDB entries from 2024-05-29

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