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1JHN

Crystal Structure of the Lumenal Domain of Calnexin

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
ASER75
AASP118
ALYS119
AASP437

Functional Information from PROSITE/UniProt
site_idPS00803
Number of Residues16
DetailsCALRETICULIN_1 Calreticulin family signature 1. NfQNgieCGGAYVKLL
ChainResidueDetails
AASN154-LEU169

site_idPS00804
Number of Residues9
DetailsCALRETICULIN_2 Calreticulin family signature 2. IMFGPDkCG
ChainResidueDetails
AILE188-GLY196

site_idPS00805
Number of Residues13
DetailsCALRETICULIN_REPEAT Calreticulin family repeated motif signature. IeDpEdqKPEDWD
ChainResidueDetails
AILE277-ASP289
AILE294-ASN306
AVAL332-ASP344

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11583625
ChainResidueDetails
ASER75
AASP118
AASP437

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:11583625
ChainResidueDetails
ATYR165
ALYS167
ATYR186
AGLU426

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14211
ChainResidueDetails
AASP193

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P27824
ChainResidueDetails
ALYS138

226707

PDB entries from 2024-10-30

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