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3RG0

Structural and functional relationships between the lectin and arm domains of 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 1
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

site_idPS00805
Number of Residues13
DetailsCALRETICULIN_REPEAT Calreticulin family repeated motif signature. IkDpDaaKPEDWD
ChainResidueDetails
AILE208-ASP220
AILE225-ASP237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20880849
ChainResidueDetails
AGLN26
ALYS62
ALYS64
AASP328

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:20880849, ECO:0007744|PDB:3O0W
ChainResidueDetails
ATYR109
ALYS111
ATYR128
AASP135
AASP317

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27797
ChainResidueDetails
ALYS48
ALYS159

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P27797
ChainResidueDetails
ALYS64

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS209

229380

PDB entries from 2024-12-25

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