Research workbench
Crystal structure of MYCP1 from mycobacterium smegmatis
Analyse Crystal structure of MYCP1 from mycobacterium smegmatis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KB5
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-anchored mycosin MYCP1
- UniProt
- A0QNL1
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane-anchored mycosin MYCP1 | protein | 386 | 24% helix, 18% strand | A0QNL1 |
Ligands and binding sites
- GOL · Glycerol · additive · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 707 | 0.70 | 0.78 | 63 | empty |
| 2 | 182 | 0.45 | 0.74 | 20 | empty |
| 3 | 111 | 0.39 | 0.75 | 23 | empty |
| 4 | 80 | 0.35 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 A0QNL1
- Elsewhere: RCSB PDB 4KB5 · PDBe 4KB5 · UniProt A0QNL1
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