MolNFT v1 · #127461 · protein
High resolution crystal structure of the mcr-2 catalytic domain
5MX9 · Phosphatidylethanolamine transferase mcr-2: “High resolution crystal structure of the mcr-2 catalytic domain”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.57). MolNFT v1 #127461 on GenesisL1: 3D structure…
- PDB
- 5MX9
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylethanolamine transferase mcr-2
- UniProt
- A0A1C3NEV1
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylethanolamine transferase mcr-2 | protein | 324 | 31% helix, 17% strand | A0A1C3NEV1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.57 | 0.90 | 21 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5MX9 · High resolution crystal structure of the MCR-2 catalytic domain · the same entry in another collection · chain A 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 A0A1C3NEV1
- Elsewhere: RCSB PDB 5MX9 · PDBe 5MX9 · UniProt A0A1C3NEV1
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