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6RP1

1.49 A RESOLUTION OF SPOROSARCINA PASTEURII UREASE INHIBITED IN THE PRESENCE OF NBPTO AT pH 6.5

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 Residues10
Detailsbinding site for residue EDO A 201
ChainResidue
AGLY50
CLYS559
ALYS51
ATHR52
APHE86
AASP88
AHOH309
AHOH343
CVAL309
CASN310

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 202
ChainResidue
AGLY27
ALYS29
AASP67
AASP68
AHOH302
AHOH305

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 203
ChainResidue
ACXM1
ATYR32
AASP79
AHOH301
AHOH303
CGLN472

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 B 201
ChainResidue
BARG116
BHOH374

site_idAC5
Number of Residues6
Detailsbinding site for residue NI C 601
ChainResidue
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
C2PA619

site_idAC6
Number of Residues5
Detailsbinding site for residue NI C 602
ChainResidue
CHIS137
CHIS139
CKCX220
CASP363
C2PA619

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO C 603
ChainResidue
CASP34
CTHR36
CTYR38
CHOH824
CHOH825
CHOH882

site_idAC8
Number of Residues5
Detailsbinding site for residue EDO C 604
ChainResidue
CASP286
CALA289
CILE537
CILE539
CHOH852

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO C 605
ChainResidue
CPRO143
CGLY189
CPRO191
CARG478
CHOH765

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO C 606
ChainResidue
CTYR93
CGLU423
CGLN501
CARG513
CILE514
CHOH897

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO C 607
ChainResidue
BPRO70
BTHR73
CGLN7
CSER11

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO C 608
ChainResidue
CLYS33
CTYR35
CHOH738

site_idAD4
Number of Residues6
Detailsbinding site for residue EDO C 609
ChainResidue
CHIS422
CGLU423
CGLY430
CGLN501
CHOH808
CHOH1040

site_idAD5
Number of Residues12
Detailsbinding site for residue EDO C 610
ChainResidue
BPRO39
BARG76
BGLU78
CALA334
CASP337
CSER338
CTYR544
CHOH702
CHOH705
CHOH711
CHOH766
CHOH850

site_idAD6
Number of Residues4
Detailsbinding site for residue EDO C 611
ChainResidue
BASP101
CPRO229
CASP233
CHOH1131

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO C 612
ChainResidue
CHIS293
CASN295

site_idAD8
Number of Residues6
Detailsbinding site for residue EDO C 613
ChainResidue
CLYS185
CLYS507
CGLY509
CHOH726
CHOH1083
CHOH1083

site_idAD9
Number of Residues9
Detailsbinding site for residue EDO C 614
ChainResidue
CPHE335
CHOH716
CHOH806
CHOH929
BHOH376
CGLY46
CLEU325
CGLU331
CASP332

site_idAE1
Number of Residues11
Detailsbinding site for residue SO4 C 615
ChainResidue
BSER71
BGLY72
BTHR73
CSER11
CTYR12
CASN43
CLYS48
CLYS326
CILE329
CHOH1051
CHOH1052

site_idAE2
Number of Residues4
Detailsbinding site for residue SO4 C 616
ChainResidue
CVAL558
CLYS559
CGLU560
CHOH1070

site_idAE3
Number of Residues7
Detailsbinding site for residue SO4 C 617
ChainResidue
CSER204
CILE205
CHOH730
CHOH773
CHOH865
CHOH971
CHOH1032

site_idAE4
Number of Residues13
Detailsbinding site for residue SO4 C 618
ChainResidue
CHIS222
CGLU223
CASP224
CHIS249
CGLY280
CLEU319
CHIS323
CARG339
CMET367
C2PA619
CHOH709
CHOH729
CHOH744

site_idAE5
Number of Residues16
Detailsbinding site for residue 2PA C 619
ChainResidue
CHIS137
CHIS139
CALA170
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
CHIS323
CASP363
CALA366
CMET367
CNI601
CNI602
CSO4618
CHOH729

site_idAE6
Number of Residues6
Detailsbinding site for residue SO4 C 620
ChainResidue
CLYS518
CLYS518
CHOH715
CHOH715
CHOH899
CHOH899

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
CHIS137
CHIS275
CASP363

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

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

226707

PDB entries from 2024-10-30

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