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6I9Y

The 2.14 A X-ray crystal structure of Sporosarcina pasteurii urease in complex with Au(I) ions

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
C0006807biological_processobsolete nitrogen compound metabolic process
C0009039molecular_functionurease activity
C0016151molecular_functionnickel cation binding
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0019627biological_processurea metabolic process
C0043419biological_processurea catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 201
ChainResidue
AGLY50
ALYS51
ATHR52
APRO87
CVAL309
CASN310
CLYS559

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 202
ChainResidue
AGLU58
CPRO330
CVAL333
CALA334
AALA54
AMET57

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 203
ChainResidue
AALA6
AGLU7
ALYS10
ATHR85
ATHR90
CPHE568
CPHE570

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 201
ChainResidue
BASP101
BHOH323
CPRO229
CEDO617

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 202
ChainResidue
APHE42
AGLU59
AHIS62
BGLU84
BHOH324

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 B 203
ChainResidue
BILE30
BARG31
BHOH317

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 B 204
ChainResidue
BARG116
BHOH307

site_idAC8
Number of Residues8
Detailsbinding site for residue NI C 601
ChainResidue
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
CNI602
COH603
CHOH713

site_idAC9
Number of Residues7
Detailsbinding site for residue NI C 602
ChainResidue
CHIS137
CHIS139
CKCX220
CASP363
CNI601
COH603
CHOH771

site_idAD1
Number of Residues9
Detailsbinding site for residue OH C 603
ChainResidue
CHIS137
CKCX220
CHIS275
CASP363
CNI601
CNI602
CHOH713
CHOH771
CHOH820

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO C 604
ChainResidue
CSER204
CILE205
CALA206

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO C 605
ChainResidue
CASP286
CILE537
CASP538
CILE539
CHOH707

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO C 606
ChainResidue
CHIS293
CASN295
CHOH755

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO C 607
ChainResidue
CPRO342
CALA346
CCYS555

site_idAD6
Number of Residues2
Detailsbinding site for residue EDO C 608
ChainResidue
BSER71
CLYS48

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO C 609
ChainResidue
CASP34
CTHR36
CTYR38
CHOH863

site_idAD8
Number of Residues5
Detailsbinding site for residue SO4 C 610
ChainResidue
CTYR35
CILE97
CGLU429
CHOH710
CHOH884

site_idAD9
Number of Residues3
Detailsbinding site for residue SO4 C 611
ChainResidue
CILE500
CARG513
CILE514

site_idAE1
Number of Residues4
Detailsbinding site for residue AU C 612
ChainResidue
CCYS322
CHIS323
CAU613
CSO4615

site_idAE2
Number of Residues4
Detailsbinding site for residue AU C 613
ChainResidue
CCYS322
CMET367
CAU612
CSO4615

site_idAE3
Number of Residues2
Detailsbinding site for residue AU C 614
ChainResidue
CGLN387
CCYS555

site_idAE4
Number of Residues11
Detailsbinding site for residue SO4 C 615
ChainResidue
CHIS323
CARG339
CAU612
CAU613
CEDO616
CHOH713
CHOH761
CHOH820
CGLU223
CASP224
CHIS249

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO C 616
ChainResidue
CGLY46
CLYS48
CASP224
CHIS323
CSO4615

site_idAE6
Number of Residues6
Detailsbinding site for residue EDO C 617
ChainResidue
BEDO201
CASP233
CARG264
CALA265
CASN267
CARG269

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
CHIS323

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
CASP363
CHIS137
CHIS275

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:30969470
ChainResidueDetails
CALA170
CHIS222
CHIS249
CALA366
CHIS139

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
CKCX220

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
CKCX220

221051

PDB entries from 2024-06-12

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