Research workbench
Crystal structure of esterase a from streptococcus pyogenes
Analyse Crystal structure of esterase a from streptococcus pyogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ROT
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase a
- EC
- 3.1.1.1, 3.1.1.2
- UniProt
- V6W522
- Ligands
- OXL, ZN
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase a (EC 3.1.1.1, 3.1.1.2) | protein | 268 | 34% helix, 21% strand | V6W522 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.47 | 0.80 | 24 | empty |
Compared structures
- 4ROT · Crystal structure of esterase A from Streptococcus pyogenes · 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 V6W522
- Elsewhere: RCSB PDB 4ROT · PDBe 4ROT · UniProt V6W522
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