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1AQR

CU-METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, MINIMIZED AVERAGE STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0010273biological_processdetoxification of copper ion
A0046870molecular_functioncadmium ion binding
A0046872molecular_functionmetal ion binding
A0071585biological_processdetoxification of cadmium ion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU1 A 41
ChainResidue
ACYS7
ACYS9
ACYS24
ACU143
ACU144
ACU147

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU1 A 42
ChainResidue
ACYS36
ACU145
ACU146
ACU147
ACYS9
ACYS11
ACYS14

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CU1 A 43
ChainResidue
ACYS7
ACYS14
ACYS20
AGLN21
ACYS24
ACYS38
ACU141
ACU147

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU1 A 44
ChainResidue
ACYS24
ASER25
ACYS26
ACYS38
ACU141
ACU146
ACU147

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CU1 A 45
ChainResidue
ACYS9
ACYS11
ACYS30
ACYS36
ACU142
ACU146

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CU1 A 46
ChainResidue
ACYS26
ACYS30
ACYS36
ACU142
ACU144
ACU145
ACU147

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CU1 A 47
ChainResidue
ACYS7
ACYS9
ACYS14
ACYS24
ACYS38
ACU141
ACU142
ACU143
ACU144
ACU146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ACYS9
ACYS11
ACYS14
ACYS20
ACYS24
ACYS26
ACYS30
ACYS36
ACYS38
ACYS7

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS22

219869

PDB entries from 2024-05-15

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