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9GOQ

Structure of the S.aureus MecA protein, in complex with ClpC

Functional Information from GO Data
ChainGOidnamespacecontents
A0030674molecular_functionprotein-macromolecule adaptor activity
B0030674molecular_functionprotein-macromolecule adaptor activity
C0030674molecular_functionprotein-macromolecule adaptor activity
D0030674molecular_functionprotein-macromolecule adaptor activity
E0030674molecular_functionprotein-macromolecule adaptor activity
F0030674molecular_functionprotein-macromolecule adaptor activity
a0000166molecular_functionnucleotide binding
a0005524molecular_functionATP binding
a0006457biological_processprotein folding
a0044183molecular_functionprotein folding chaperone
a1990169biological_processstress response to copper ion
a1990170biological_processstress response to cadmium ion
b0000166molecular_functionnucleotide binding
b0005524molecular_functionATP binding
b0006457biological_processprotein folding
b0044183molecular_functionprotein folding chaperone
b1990169biological_processstress response to copper ion
b1990170biological_processstress response to cadmium ion
c0000166molecular_functionnucleotide binding
c0005524molecular_functionATP binding
c0006457biological_processprotein folding
c0044183molecular_functionprotein folding chaperone
c1990169biological_processstress response to copper ion
c1990170biological_processstress response to cadmium ion
d0000166molecular_functionnucleotide binding
d0005524molecular_functionATP binding
d0006457biological_processprotein folding
d0044183molecular_functionprotein folding chaperone
d1990169biological_processstress response to copper ion
d1990170biological_processstress response to cadmium ion
e0000166molecular_functionnucleotide binding
e0005524molecular_functionATP binding
e0006457biological_processprotein folding
e0044183molecular_functionprotein folding chaperone
e1990169biological_processstress response to copper ion
e1990170biological_processstress response to cadmium ion
f0000166molecular_functionnucleotide binding
f0005524molecular_functionATP binding
f0006457biological_processprotein folding
f0044183molecular_functionprotein folding chaperone
f1990169biological_processstress response to copper ion
f1990170biological_processstress response to cadmium ion
g0000166molecular_functionnucleotide binding
g0005524molecular_functionATP binding
g0006457biological_processprotein folding
g0044183molecular_functionprotein folding chaperone
g1990169biological_processstress response to copper ion
g1990170biological_processstress response to cadmium ion
h0000166molecular_functionnucleotide binding
h0005524molecular_functionATP binding
h0006457biological_processprotein folding
h0044183molecular_functionprotein folding chaperone
h1990169biological_processstress response to copper ion
h1990170biological_processstress response to cadmium ion
i0000166molecular_functionnucleotide binding
i0005524molecular_functionATP binding
i0006457biological_processprotein folding
i0044183molecular_functionprotein folding chaperone
i1990169biological_processstress response to copper ion
i1990170biological_processstress response to cadmium ion
l0000166molecular_functionnucleotide binding
l0005524molecular_functionATP binding
l0006457biological_processprotein folding
l0044183molecular_functionprotein folding chaperone
l1990169biological_processstress response to copper ion
l1990170biological_processstress response to cadmium ion
m0000166molecular_functionnucleotide binding
m0005524molecular_functionATP binding
m0006457biological_processprotein folding
m0044183molecular_functionprotein folding chaperone
m1990169biological_processstress response to copper ion
m1990170biological_processstress response to cadmium ion
n0000166molecular_functionnucleotide binding
n0005524molecular_functionATP binding
n0006457biological_processprotein folding
n0044183molecular_functionprotein folding chaperone
n1990169biological_processstress response to copper ion
n1990170biological_processstress response to cadmium ion
Functional Information from PROSITE/UniProt
site_idPS00870
Number of Residues13
DetailsCLPAB_1 Chaperonins clpA/B signature 1. DASNILKPaLarG
ChainResidueDetails
aASP295-GLY307

site_idPS00871
Number of Residues19
DetailsCLPAB_2 Chaperonins clpA/B signature 2. RVDmSEFmEKhAvSRLvGA
ChainResidueDetails
aARG571-ALA589

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PDB entries from 2026-01-14

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