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2E69

Crystal structure of the stationary phase survival protein SurE from Thermus thermophilus HB8 in complex with sulfate

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AASP8
AASN96
AASN100
ASER108
AGLY109
ATHR110
AHOH417

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ASER178
AVAL179
AARG180
ATYR182
AARG214
AHOH460
AGLY102
AHIS103

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG180
AHOH426

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG228
ALEU229
AASP230
AHOH455
AHOH467
BHOH432

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ATHR235
AARG236
APRO239
ATHR240
AHOH406

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 306
ChainResidue
BASP8
BASN96
BASN100
BSER108
BGLY109
BTHR110
BHOH426

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 307
ChainResidue
BGLY102
BHIS103
BSER178
BARG180
BTYR182
BARG214
BHOH430

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 308
ChainResidue
BARG180
BHOH434

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 309
ChainResidue
AILE45
AGLN116
BHIS103
BPRO202

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 310
ChainResidue
CASP8
CASN96
CASN100
CSER108
CGLY109
CTHR110
CHOH327

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 311
ChainResidue
CGLY102
CHIS103
CSER178
CARG180
CTYR182
CARG214
CHOH317

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 312
ChainResidue
DASP8
DASN96
DASN100
DSER108
DGLY109
DTHR110
DHOH323

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 313
ChainResidue
DGLY102
DHIS103
DSER178
DVAL179
DARG180
DTYR182
DARG214
DHOH355

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 314
ChainResidue
DARG180
DHOH334

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
ASER24
AGLY27
AGLU28
AVAL29
APRO66

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 402
ChainResidue
BGLU28
BVAL29
BPRO55
BHIS64
BHOH424

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. NLGHEIWHSG
ChainResidueDetails
AASN100-GLY109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00060
ChainResidueDetails
AASP8
CASP9
CSER39
CASN96
DASP8
DASP9
DSER39
DASN96
AASP9
ASER39
AASN96
BASP8
BASP9
BSER39
BASN96
CASP8

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PDB entries from 2024-04-24

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