4MT2
COMPARISON OF THE NMR SOLUTION STRUCTURE AND THE X-RAY CRYSTAL STRUCTURE OF RAT METALLOTHIONEIN-2
Replaces: 2MT2Replaces: 1MT2Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006882 | biological_process | intracellular zinc ion homeostasis |
| A | 0007263 | biological_process | nitric oxide mediated signal transduction |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009617 | biological_process | response to bacterium |
| A | 0010273 | biological_process | detoxification of copper ion |
| A | 0036016 | biological_process | cellular response to interleukin-3 |
| A | 0036018 | biological_process | cellular response to erythropoietin |
| A | 0045926 | biological_process | negative regulation of growth |
| A | 0046870 | molecular_function | cadmium ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048143 | biological_process | astrocyte activation |
| A | 0071276 | biological_process | cellular response to cadmium ion |
| A | 0071280 | biological_process | cellular response to copper ion |
| A | 0071294 | biological_process | cellular response to zinc ion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 62 |
| Chain | Residue |
| A | CYS50 |
| A | CYS57 |
| A | CYS59 |
| A | CYS60 |
| A | CD65 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 63 |
| Chain | Residue |
| A | CYS33 |
| A | CYS34 |
| A | CYS44 |
| A | CYS48 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 64 |
| Chain | Residue |
| A | CYS37 |
| A | CYS41 |
| A | CYS44 |
| A | CYS60 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 65 |
| Chain | Residue |
| A | CYS34 |
| A | CYS36 |
| A | CYS37 |
| A | CYS50 |
| A | CD62 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 66 |
| Chain | Residue |
| A | CYS5 |
| A | CYS7 |
| A | CYS21 |
| A | CYS24 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 67 |
| Chain | Residue |
| A | CYS15 |
| A | CYS19 |
| A | CYS24 |
| A | CYS29 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 68 |
| Chain | Residue |
| A | CYS7 |
| A | CYS13 |
| A | CYS15 |
| A | CYS26 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 69 |
| Chain | Residue |
| A | CYS29 |
| A | ALA42 |
| A | SER45 |
| A | HOH70 |
| A | HOH71 |
| A | HOH72 |
Functional Information from PROSITE/UniProt
| site_id | PS00203 |
| Number of Residues | 19 |
| Details | METALLOTHIONEIN_VRT Vertebrate metallothioneins signature. CsCAgsCkCkqCkCtsCkK |
| Chain | Residue | Details |
| A | CYS13-LYS31 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Region: {"description":"Beta"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1942051","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3184190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2MRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MT2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1942051","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3184190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MT2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"6470004","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
