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1ZKC

Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 638
ChainResidue
AASN327
AARG385
ASER386
ACYS387
AVAL455

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME B 639
ChainResidue
BCYS387
BVAL455
BASN327
BPHE328
BARG385
BSER386

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YdgTiFHRSIrnFViQGG
ChainResidueDetails
ATYR316-GLY333

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PDB entries from 2024-11-06

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