Research workbench
Comparison of the NMR solution structure and the X-ray crystal structure of rat metallothionein-2
Analyse Comparison of the NMR solution structure and the X-ray crystal structure of rat… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MT2
- Type
- protein
- Length
- 61 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallothionein isoform II
- UniProt
- P04355
- Ligands
- ACE, CD, ZN, NA
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallothionein isoform II | protein | 61 | 0% helix, 0% strand | P04355 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- CD · Cadmium ion · metal · 5 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4MT2 · Comparison of the NMR solution structure and the X-ray crystal structure of rat… · the same entry in another collection · chain A against A, TM-score 1.00
- P04355 · AlphaFold monomer V2.0 prediction for metallothionein-2 (P04355) · a predicted model of the same protein · chain A against A, TM-score 0.47
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04355
- Elsewhere: RCSB PDB 4MT2 · PDBe 4MT2 · UniProt P04355
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