Research workbench
Crystal structure of MYCP1 with the N-terminal propeptide removed
Analyse Crystal structure of MYCP1 with the N-terminal propeptide removed in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M1Z
- Type
- protein
- Length
- 655 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane-anchored mycosin MYCP1
- EC
- 3.4.21.62
- UniProt
- A0QNL1
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 4 distinct chains · 26% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane-anchored mycosin MYCP1 (EC 3.4.21.62) | protein | 317 | 27% helix, 22% strand | A0QNL1 |
| B | Membrane-anchored mycosin MYCP1 (EC 3.4.21.62) | protein | 315 | 28% helix, 22% strand | A0QNL1 |
| C | Membrane-anchored mycosin MYCP1 | protein | 10 | 0% helix, 10% strand | A0QNL1 |
| D | Membrane-anchored mycosin MYCP1 | protein | 13 | 0% helix, 8% strand | A0QNL1 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 407 | 0.58 | 0.75 | 56 | empty |
| 2 | 341 | 0.56 | 0.75 | 38 | empty |
| 3 | 330 | 0.54 | 0.74 | 33 | empty |
| 4 | 188 | 0.51 | 0.77 | 24 | empty |
| 5 | 65 | 0.31 | 0.75 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 632 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 536 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 486 Ų buried · 8 hydrogen bonds · protein-protein
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 4M1Z · PDBe 4M1Z · UniProt A0QNL1
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