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5GHU

Crystal structure of YadV chaperone at 1.63 Angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0043711biological_processpilus organization
A0061077biological_processchaperone-mediated protein folding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 301
ChainResidue
AARG9
ALYS119
AILE209

site_idAC2
Number of Residues1
Detailsbinding site for residue ACT A 302
ChainResidue
AHOH426

site_idAC3
Number of Residues2
Detailsbinding site for residue FMT A 304
ChainResidue
AGLN34
AGLN34

site_idAC4
Number of Residues4
Detailsbinding site for residue PGE A 305
ChainResidue
AHOH413
AASP83
APHE212
AHOH405

Functional Information from PROSITE/UniProt
site_idPS00635
Number of Residues18
DetailsPILI_CHAPERONE Gram-negative pili assembly chaperone signature. LPkDRESVfWfNVleVPP
ChainResidueDetails
ALEU80-PRO97

219515

PDB entries from 2024-05-08

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