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4R3E

Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AARG56
AALA102
AASN103
APHE114
AHIS127
AHOH608
AHOH609
AHOH666

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
ASER89
AALA102
AASN103
AASP108
AGLY110
AGLN112
AGOL403
AHOH539
AHOH540
AHOH665
AHOH666
AGLN64

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AGLY72
ASER73
AHIS88
ASER89
AGOL402
AHOH598

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YdnTiFHRVVpgFIvQGG
ChainResidueDetails
ATYR49-GLY66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues155
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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