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4TNS

Structure of Pin1 PPIase domain bound with all-trans retinoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue REA A 201
ChainResidue
AHIS59
ASER154
AHIS157
AHOH305
AHOH341
BHOH223
ALYS63
AARG68
AARG69
ASER71
AASP112
AMET130
AGLN131
APHE134

Functional Information from PROSITE/UniProt
site_idPS01096
Number of Residues21
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG
ChainResidueDetails
APHE103-GLY123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER43
BSER43

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS46
BLYS46

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by DAPK1 => ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:29686383
ChainResidueDetails
ASER71
BSER71

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
ASER108
BSER108

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 511
ChainResidueDetails
AHIS59proton shuttle (general acid/base)
ACYS113covalently attached, electrostatic stabiliser
AGLN131electrostatic stabiliser
ASER154electrostatic stabiliser
AHIS157electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 511
ChainResidueDetails
BHIS59proton shuttle (general acid/base)
BCYS113covalently attached, electrostatic stabiliser
BGLN131electrostatic stabiliser
BSER154electrostatic stabiliser
BHIS157electrostatic stabiliser

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PDB entries from 2024-04-24

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