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The crystal structure of a M20 family metallo-carboxypeptidase sso-CP2 from sulfolobus solfataricus
Analyse The crystal structure of a M20 family metallo-carboxypeptidase sso-CP2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MMO
- Type
- protein
- Length
- 819 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sso-CP2 metallo-carboxypetidase
- UniProt
- Q97V97
- Ligands
- ZN, SO4
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sso-CP2 metallo-carboxypetidase | protein | 437 | 36% helix, 22% strand | Q97V97 |
| B | Sso-CP2 metallo-carboxypetidase | protein | 382 | 36% helix, 22% strand | Q97V97 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1179 | 0.79 | 0.81 | 86 | SO4 |
| 2 | 180 | 0.67 | 0.86 | 42 | empty |
| 3 | 202 | 0.65 | 0.84 | 36 | empty |
| 4 | 185 | 0.58 | 0.81 | 22 | empty |
| 5 | 135 | 0.50 | 0.79 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 2810 Ų buried · 56 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4MMO · The crystal structure of a M20 family metallo-carboxypeptidase Sso-CP2 from Sulfolobus… · 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 Q97V97
- Elsewhere: RCSB PDB 4MMO · PDBe 4MMO · UniProt Q97V97
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