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4CEX

1.59 A resolution Fluoride 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
CF1571
CF1572

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NI C 601
ChainResidue
CHIS139
CKCX220
CASP363
CNI600
CF1571
CF1572
CHOH2189
CHIS137

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE F C 1571
ChainResidue
CHIS137
CKCX220
CHIS275
CASP363
CNI600
CNI601
CF1572
CHOH2189
CHOH2297

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE F C 1572
ChainResidue
CALA170
CKCX220
CHIS222
CHIS249
CNI600
CNI601
CF1571
CHOH2189

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 1573
ChainResidue
CASP34
CTHR36
CTYR38
CHOH2057
CHOH2071
CHOH2510

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 1101
ChainResidue
AGLY50
ALYS51
ATHR52
APHE86
AASP88
AHOH2124
AHOH2125
CVAL309
CASN310
CLYS559

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 1574
ChainResidue
CASP286
CALA289
CILE537
CILE539
CHOH2279
CHOH2479

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 1575
ChainResidue
BHOH2101
CGLY46
CLEU325
CASP332
CPHE335
CHOH2245
CHOH2333

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1127
ChainResidue
BASP101
BHOH2157
CPRO229
CHOH2255
CHOH2287

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 1576
ChainResidue
CTYR93
CGLU423
CGLN501
CARG513
CILE514
CHOH2432
CHOH2512

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 1577
ChainResidue
CTYR35
CTYR83
CILE97
CGLU429
CHOH2055
CHOH2513
CHOH2514

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1102
ChainResidue
AGLY27
ALYS29
AASP67
AASP68
AHOH2044
AHOH2051

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 1578
ChainResidue
CARG62
CPRO177
CTRP178
CGLU181
CHOH2515

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1103
ChainResidue
CHOH2352
AASN4
AALA6
ALYS10
AHOH2111
AHOH2126
CPHE568
CPHE570

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1128
ChainResidue
BASN68
BILE69
BGLU86
BHOH2138
CMET1

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1129
ChainResidue
BARG116
BHOH2174

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1579
ChainResidue
CVAL558
CLYS559
CGLU560
CHOH2500
CHOH2516
CHOH2517

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1580
ChainResidue
CLYS511
CLYS511
CLYS511
CHOH2518
CHOH2518
CHOH2518

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

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PDB entries from 2024-10-30

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