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3POW

Crystal structure of the globular domain of human calreticulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005783cellular_componentendoplasmic reticulum
A0006457biological_processprotein folding
A0051082molecular_functionunfolded protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 900
ChainResidue
AGLN26
ALYS62
ALYS64
AASP328

Functional Information from PROSITE/UniProt
site_idPS00803
Number of Residues16
DetailsCALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF
ChainResidueDetails
ALYS98-PHE113

site_idPS00804
Number of Residues9
DetailsCALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG
ChainResidueDetails
AILE130-GLY138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsRepeat: {"description":"1-1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues179
DetailsRegion: {"description":"N-domain"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21423620","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27840680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3POS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3POW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LK5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14211","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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