Research workbench
Crystal structure of the ADP conformation of MJ1267, an ATP- binding cassette of an ABC transporter
Analyse Crystal structure of the ADP conformation of MJ1267, an ATP- binding cassette… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G6H
- Type
- protein
- Length
- 254 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High-affinity branched-chain amino acid transport ATP-binding protein
- UniProt
- Q58663
- Ligands
- MMC, ADP, MG
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High-affinity branched-chain amino acid transport ATP-binding protein | protein | 254 | 40% helix, 25% strand | Q58663 |
Ligands and binding sites
- MMC · Methyl mercury ion · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.42 | 0.80 | 12 | empty |
| 2 | 80 | 0.34 | 0.74 | 10 | empty |
| 3 | 56 | 0.31 | 0.76 | 15 | empty |
Compared structures
- 1G6H · Crystal structure of the ADP conformation of MJ1267, an ATP-binding cassette of an ABC… · the same entry in another collection · chain A against A, TM-score 1.00
- Q58663 · AlphaFold monomer V2.0 prediction for probable branched-chain amino acid transport… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q58663
- Elsewhere: RCSB PDB 1G6H · PDBe 1G6H · UniProt Q58663
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.