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8XUD

Crystal structure of adaptor NlpI in complex with endopeptidase MepS and PDZ-protease Prc

Functional Information from GO Data
ChainGOidnamespacecontents
A0000270biological_processpeptidoglycan metabolic process
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0030674molecular_functionprotein-macromolecule adaptor activity
A0042803molecular_functionprotein homodimerization activity
A0051301biological_processcell division
B0000270biological_processpeptidoglycan metabolic process
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0030674molecular_functionprotein-macromolecule adaptor activity
B0042803molecular_functionprotein homodimerization activity
B0051301biological_processcell division
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
D0006508biological_processproteolysis
D0008236molecular_functionserine-type peptidase activity
I0000270biological_processpeptidoglycan metabolic process
I0004175molecular_functionendopeptidase activity
I0005515molecular_functionprotein binding
I0006508biological_processproteolysis
I0008233molecular_functionpeptidase activity
I0008234molecular_functioncysteine-type peptidase activity
I0009254biological_processpeptidoglycan turnover
I0009279cellular_componentcell outer membrane
I0016787molecular_functionhydrolase activity
I0045227biological_processcapsule polysaccharide biosynthetic process
I0071555biological_processcell wall organization
I0106415molecular_functionmuramoyltetrapeptide carboxypeptidase activity
J0000270biological_processpeptidoglycan metabolic process
J0004175molecular_functionendopeptidase activity
J0005515molecular_functionprotein binding
J0006508biological_processproteolysis
J0008233molecular_functionpeptidase activity
J0008234molecular_functioncysteine-type peptidase activity
J0009254biological_processpeptidoglycan turnover
J0009279cellular_componentcell outer membrane
J0016787molecular_functionhydrolase activity
J0045227biological_processcapsule polysaccharide biosynthetic process
J0071555biological_processcell wall organization
J0106415molecular_functionmuramoyltetrapeptide carboxypeptidase activity
K0000270biological_processpeptidoglycan metabolic process
K0004175molecular_functionendopeptidase activity
K0005515molecular_functionprotein binding
K0006508biological_processproteolysis
K0008233molecular_functionpeptidase activity
K0008234molecular_functioncysteine-type peptidase activity
K0009254biological_processpeptidoglycan turnover
K0009279cellular_componentcell outer membrane
K0016787molecular_functionhydrolase activity
K0045227biological_processcapsule polysaccharide biosynthetic process
K0071555biological_processcell wall organization
K0106415molecular_functionmuramoyltetrapeptide carboxypeptidase activity
L0000270biological_processpeptidoglycan metabolic process
L0004175molecular_functionendopeptidase activity
L0005515molecular_functionprotein binding
L0006508biological_processproteolysis
L0008233molecular_functionpeptidase activity
L0008234molecular_functioncysteine-type peptidase activity
L0009254biological_processpeptidoglycan turnover
L0009279cellular_componentcell outer membrane
L0016787molecular_functionhydrolase activity
L0045227biological_processcapsule polysaccharide biosynthetic process
L0071555biological_processcell wall organization
L0106415molecular_functionmuramoyltetrapeptide carboxypeptidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues66
DetailsRepeat: {"description":"TPR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15634341","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsRepeat: {"description":"TPR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15634341","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsRepeat: {"description":"TPR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15634341","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues168
DetailsDomain: {"description":"PDZ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00143","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues30
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues484
DetailsDomain: {"description":"NlpC/P60","evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-12-03

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