MolNFT v1 · #10282 · protein
Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis
1IMD: “Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis”. X-ray diffraction. MolNFT v1 #10282 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1IMD
- Type
- protein
- Length
- 538 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29218
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 266 | — | P29218 |
| B | — | protein | 272 | — | P29218 |
Compared structures
- 1IMD · Structural studies of metal binding by inositol monophosphatase: evidence for two-metal… · the same entry in another collection · chain A against A, TM-score 1.00
- P29218 · AlphaFold monomer V2.0 prediction for inositol monophosphatase 1 (P29218) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P29218
- Elsewhere: RCSB PDB 1IMD · PDBe 1IMD · UniProt P29218
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.