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3CJK

Crystal structure of the adduct HAH1-Cd(II)-MNK1.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006811biological_processmonoatomic ion transport
A0006825biological_processcopper ion transport
A0006878biological_processintracellular copper ion homeostasis
A0006979biological_processresponse to oxidative stress
A0016530molecular_functionmetallochaperone activity
A0016531molecular_functioncopper chaperone activity
A0032767molecular_functioncopper-dependent protein binding
A0043066biological_processnegative regulation of apoptotic process
A0046872molecular_functionmetal ion binding
A0051117molecular_functionATPase binding
A0060003biological_processcopper ion export
A1903136molecular_functioncuprous ion binding
B0005507molecular_functioncopper ion binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD B 1
ChainResidue
ACYS12
BTHR14
BCYS15
BCYS18

Functional Information from PROSITE/UniProt
site_idPS01047
Number of Residues30
DetailsHMA_1 Heavy-metal-associated domain. VeGMtCnSCvwtIEqqIgkvngvhhik.VsL
ChainResidueDetails
BVAL10-LEU39
ASER7-LEU35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31283225, ECO:0007744|PDB:5T7L
ChainResidueDetails
BTHR14
ACYS15

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:31283225, ECO:0007744|PDB:5T7L
ChainResidueDetails
BCYS15
BCYS18

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08997
ChainResidueDetails
ALYS60

237735

PDB entries from 2025-06-18

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