MolNFT v1 · #140772 · protein
Crystal structure of mcr-1 catalytic domain
5YLC · Probable phosphatidylethanolamine transferase mcr-1: “Crystal structure of mcr-1 catalytic domain”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.51). MolNFT v1 #140772 on GenesisL1: 3D structure, binding sites…
- PDB
- 5YLC
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable phosphatidylethanolamine transferase mcr-1
- EC
- 2.7.-.-
- UniProt
- A0A0R6L508
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable phosphatidylethanolamine transferase mcr-1 (EC 2.7.-.-) | protein | 330 | 32% helix, 17% strand | A0A0R6L508 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.51 | 0.87 | 22 | empty |
| 2 | 97 | 0.42 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 modified (disulfide, phosphorylation).
Compared structures
- 5YLC · Crystal Structure of MCR-1 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 A0A0R6L508
- Elsewhere: RCSB PDB 5YLC · PDBe 5YLC · UniProt A0A0R6L508
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