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4MT2

COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2

Replaces:  2MT2Replaces:  1MT2
Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006882biological_processintracellular zinc ion homeostasis
A0008270molecular_functionzinc ion binding
A0010273biological_processdetoxification of copper ion
A0045926biological_processnegative regulation of growth
A0046872molecular_functionmetal ion binding
A0071276biological_processcellular response to cadmium ion
A0071280biological_processcellular response to copper ion
A0071294biological_processcellular response to zinc ion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 62
ChainResidue
ACYS50
ACYS57
ACYS59
ACYS60
ACD65

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 63
ChainResidue
ACYS33
ACYS34
ACYS44
ACYS48

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 64
ChainResidue
ACYS37
ACYS41
ACYS44
ACYS60

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 65
ChainResidue
ACYS34
ACYS36
ACYS37
ACYS50
ACD62

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 66
ChainResidue
ACYS5
ACYS7
ACYS21
ACYS24

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 67
ChainResidue
ACYS15
ACYS19
ACYS24
ACYS29

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 68
ChainResidue
ACYS7
ACYS13
ACYS15
ACYS26

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 69
ChainResidue
ACYS29
AALA42
ASER45
AHOH70
AHOH71
AHOH72

Functional Information from PROSITE/UniProt
site_idPS00203
Number of Residues19
DetailsMETALLOTHIONEIN_VRT Vertebrate metallothioneins signature. CsCAgsCkCkqCkCtsCkK
ChainResidueDetails
ACYS13-LYS31

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:1942051, ECO:0000269|PubMed:3184190, ECO:0007744|PDB:2MRT, ECO:0007744|PDB:4MT2
ChainResidueDetails
ACYS5
ACYS7
ACYS13
ACYS15
ACYS19
ACYS21
ACYS24
ACYS26
ACYS29

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:1942051, ECO:0000269|PubMed:3184190, ECO:0007744|PDB:1MRT, ECO:0007744|PDB:4MT2
ChainResidueDetails
ACYS33
ACYS59
ACYS60
ACYS34
ACYS36
ACYS37
ACYS41
ACYS44
ACYS48
ACYS50
ACYS57

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:6470004
ChainResidueDetails
AMET1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02795
ChainResidueDetails
ASER58

218853

PDB entries from 2024-04-24

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