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6RKG

1.32 A RESOLUTION OF SPOROSARCINA PASTEURII UREASE INHIBITED IN THE PRESENCE OF NBPTO AT pH 7.5

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
C0006807biological_processnitrogen 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 Residues10
Detailsbinding site for residue EDO A 201
ChainResidue
AGLY50
CLYS559
ALYS51
ATHR52
APHE86
APRO87
AASP88
AHOH306
CVAL309
CASN310

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 202
ChainResidue
AASN4
AALA6
ALYS10
AHOH303
AHOH313
CPHE568
CPHE570
CHOH898

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 203
ChainResidue
AGLY27
ALYS29
AASP67
AASP68
AHOH304
AHOH315

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 204
ChainResidue
ACXM1
ATYR32
AASP79
AHOH348

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 205
ChainResidue
APHE42
AGLU59
AHOH318
AHOH334
AHOH355
BGLU84

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO B 201
ChainResidue
BASP101
CPRO229
CHOH957
CHOH1113
CHOH1163

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 B 202
ChainResidue
BARG116
BHOH385

site_idAC8
Number of Residues6
Detailsbinding site for residue NI C 601
ChainResidue
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
C2PA617

site_idAC9
Number of Residues5
Detailsbinding site for residue NI C 602
ChainResidue
CHIS137
CHIS139
CKCX220
CASP363
C2PA617

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO C 603
ChainResidue
CASP34
CTHR36
CTYR38
CHOH726
CHOH753
CHOH996

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO C 604
ChainResidue
BPRO70
BTHR73
CGLN7
CSER11
CHOH744
CHOH782

site_idAD3
Number of Residues7
Detailsbinding site for residue EDO C 605
ChainResidue
CASP286
CALA289
CILE537
CILE539
CHOH808
CHOH867
CHOH936

site_idAD4
Number of Residues7
Detailsbinding site for residue EDO C 606
ChainResidue
CTYR93
CGLU423
CGLN501
CARG513
CILE514
CHOH703
CHOH1119

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO C 607
ChainResidue
CLYS33
CTYR35
CEDO613
CHOH732

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO C 608
ChainResidue
CASP536
CASP538
CLYS547
CASP549
CGLY550

site_idAD7
Number of Residues7
Detailsbinding site for residue EDO C 609
ChainResidue
BPRO39
BARG76
BGLU78
CASP337
CSER338
CTYR544
CHOH748

site_idAD8
Number of Residues6
Detailsbinding site for residue EDO C 610
ChainResidue
CHOH900
CTYR35
CTYR83
CILE97
CGLU429
CHOH757

site_idAD9
Number of Residues3
Detailsbinding site for residue EDO C 611
ChainResidue
CPRO143
CGLY189
CARG478

site_idAE1
Number of Residues4
Detailsbinding site for residue EDO C 612
ChainResidue
CVAL309
CPRO557
CHOH911
CHOH1132

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO C 613
ChainResidue
CASP34
CTYR35
CEDO607
CHOH753

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO C 614
ChainResidue
AHIS96
CASP317
CGLN327
CHOH714

site_idAE4
Number of Residues6
Detailsbinding site for residue SO4 C 615
ChainResidue
CASN65
CSER204
CILE205
CHOH989
CHOH1006
CHOH1007

site_idAE5
Number of Residues5
Detailsbinding site for residue SO4 C 616
ChainResidue
CVAL558
CLYS559
CGLU560
CHOH999
CHOH1021

site_idAE6
Number of Residues14
Detailsbinding site for residue 2PA C 617
ChainResidue
CHIS137
CHIS139
CALA170
CKCX220
CHIS222
CHIS249
CHIS275
CGLY280
CHIS323
CASP363
CALA366
CMET367
CNI601
CNI602

site_idAE7
Number of Residues8
Detailsbinding site for residue SO4 C 618
ChainResidue
BSER71
BGLY72
CSER11
CTYR12
CASN43
CLYS48
CLYS326
CILE329

site_idAE8
Number of Residues3
Detailsbinding site for residue SO4 C 619
ChainResidue
CLYS511
CLYS511
CLYS511

site_idAE9
Number of Residues5
Detailsbinding site for residue SO4 C 620
ChainResidue
CLYS518
CLYS518
CHOH709
CHOH709
CHOH718

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

217705

PDB entries from 2024-03-27

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