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6VJ6

2.55 Angstrom Resolution Crystal Structure of Peptidylprolyl Isomerase (PrsA) from Bacillus cereus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue 2NV A 301
ChainResidue
AVAL190
APHE213
AHIS216
AHOH450

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 302
ChainResidue
ALYS128
ATYR131
ATYR229

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 303
ChainResidue
AGLU56
AASN48
ATYR49

site_idAC4
Number of Residues7
Detailsbinding site for residue 2NV B 301
ChainResidue
BASP171
BGLY187
BMSE189
BVAL190
BPHE213
BHIS216
BHOH412

Functional Information from PROSITE/UniProt
site_idPS01096
Number of Residues22
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FAaLAkqySedpgSkek..GGeLS
ChainResidueDetails
APHE161-SER182

224201

PDB entries from 2024-08-28

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