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5FSE

2.07 A resolution 1,4-Benzoquinone inhibited Sporosarcina pasteurii urease

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009039molecular_functionurease activity
A0016151molecular_functionnickel cation binding
A0016787molecular_functionhydrolase activity
A0019627biological_processurea metabolic process
A0043419biological_processurea catabolic process
B0005737cellular_componentcytoplasm
B0009039molecular_functionurease activity
B0016787molecular_functionhydrolase activity
B0035550cellular_componenturease complex
B0043419biological_processurea catabolic process
C0005737cellular_componentcytoplasm
C0009039molecular_functionurease activity
C0016151molecular_functionnickel cation binding
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0043419biological_processurea catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NI C 600
ChainResidue
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
CNI601
COH1580
CHOH2111

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NI C 601
ChainResidue
CHIS139
CKCX220
CASP363
CNI600
COH1580
CHOH2094
CHIS137

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1101
ChainResidue
AGLY50
ALYS51
ATHR52
AASP88
CVAL309
CASN310
CLYS559

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1571
ChainResidue
CASP286
CALA289
CILE537
CASP538
CILE539

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 1127
ChainResidue
BVAL85
BGLU86

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 1572
ChainResidue
CTHR37
CTYR38
CEDO1575
CHOH2293

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1573
ChainResidue
CTYR60
CASN65
CILE114
CSO41582
CHOH2081

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 1574
ChainResidue
CPRO143
CGLY189
CARG478
CHOH2119

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1575
ChainResidue
CASP34
CTHR36
CTYR38
CEDO1572
CHOH2026

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 1576
ChainResidue
CILE500
CARG513
CILE514
CHOH2295

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 1577
ChainResidue
CASP34
CTYR35
CSO41581
CHOH2026

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1578
ChainResidue
CTYR93
CGLU423
CGLN501
CARG513
CILE514

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 1579
ChainResidue
CHIS222
CHIS249
CGLY280
CHIS323
CARG339
CHOH2111
CHOH2134
CHOH2172

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OH C 1580
ChainResidue
CHIS137
CKCX220
CHIS275
CASP363
CNI600
CNI601
CHOH2094
CHOH2111
CHOH2172

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1128
ChainResidue
BLEU112
BARG116

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1581
ChainResidue
CLYS33
CTYR35
CEDO1577
CHOH2297

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 1582
ChainResidue
CSER204
CILE205
CEDO1573
CHOH2123

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE HQE C 1583
ChainResidue
CGLN387
CARG388
CTHR554
CCYS555
CGLU556
CSO41588
CHOH2298

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HQE C 1584
ChainResidue
CTHR470
CHOH2108
CHOH2110
AGLN81
CVAL321
CCYS322
CILE468
CPRO469

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1585
ChainResidue
CVAL558
CLYS559
CGLU560

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1102
ChainResidue
AMET70
AGLU71

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1586
ChainResidue
CASP107
CGLY108
CHOH2077

site_idCC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1587
ChainResidue
BSER71
BGLY72
CTYR12
CLYS48
CHOH2008
CHOH2299

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1588
ChainResidue
CARG388
CHQE1583
CHOH2300

Functional Information from PROSITE/UniProt
site_idPS00145
Number of Residues17
DetailsUREASE_2 Urease active site. MVCHHLkqnIpeDVaFA
ChainResidueDetails
CMET320-ALA336

site_idPS01120
Number of Residues14
DetailsUREASE_1 Urease nickel ligands signature. TAGGIDtHVHfinP
ChainResidueDetails
CTHR130-PRO143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
CHIS324

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
ChainResidueDetails
CVAL138
CVAL276
CALA364

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:30969470
ChainResidueDetails
CPHE140
CTHR171
CGLU223
CSER250
CMET367

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
ChainResidueDetails
CILE221

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP
ChainResidueDetails
CILE221

237735

PDB entries from 2025-06-18

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