Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1M5Y

Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0006457biological_processprotein folding
A0016853molecular_functionisomerase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0036506biological_processmaintenance of unfolded protein
A0042277molecular_functionpeptide binding
A0042597cellular_componentperiplasmic space
A0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0060274biological_processmaintenance of stationary phase
A0061077biological_processchaperone-mediated protein folding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0006457biological_processprotein folding
B0016853molecular_functionisomerase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0036506biological_processmaintenance of unfolded protein
B0042277molecular_functionpeptide binding
B0042597cellular_componentperiplasmic space
B0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0060274biological_processmaintenance of stationary phase
B0061077biological_processchaperone-mediated protein folding
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005515molecular_functionprotein binding
C0006457biological_processprotein folding
C0016853molecular_functionisomerase activity
C0030288cellular_componentouter membrane-bounded periplasmic space
C0036506biological_processmaintenance of unfolded protein
C0042277molecular_functionpeptide binding
C0042597cellular_componentperiplasmic space
C0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0060274biological_processmaintenance of stationary phase
C0061077biological_processchaperone-mediated protein folding
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0005515molecular_functionprotein binding
D0006457biological_processprotein folding
D0016853molecular_functionisomerase activity
D0030288cellular_componentouter membrane-bounded periplasmic space
D0036506biological_processmaintenance of unfolded protein
D0042277molecular_functionpeptide binding
D0042597cellular_componentperiplasmic space
D0043165biological_processGram-negative-bacterium-type cell outer membrane assembly
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0060274biological_processmaintenance of stationary phase
D0061077biological_processchaperone-mediated protein folding
Functional Information from PROSITE/UniProt
site_idPS01096
Number of Residues21
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FGkLAiahSadq.Qaln..GGqMG
ChainResidueDetails
APHE212-GLY232
APHE321-GLY342

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon