Research workbench
Crystal structure of ahpc with active site cysteine mutated to serine (C46S)
Analyse Crystal structure of ahpc with active site cysteine mutated to serine (C46S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N8J
- Type
- protein
- Length
- 3,720 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkyl hydroperoxide reductase C22 protein
- EC
- 1.11.1.15
- UniProt
- P0A251
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T | Alkyl hydroperoxide reductase C22 protein (EC 1.11.1.15) | protein | 186 | 30% helix, 28% strand | P0A251 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.67 | 0.92 | 18 | empty |
| 2 | 74 | 0.67 | 0.92 | 18 | empty |
| 3 | 90 | 0.65 | 0.90 | 18 | empty |
| 4 | 76 | 0.65 | 0.91 | 18 | empty |
| 5 | 77 | 0.64 | 0.91 | 18 | empty |
Interfaces
48 interfaces between chains.
- K–L · 2047 Ų buried · 34 hydrogen bonds · protein-protein
- Q–R · 2035 Ų buried · 33 hydrogen bonds · protein-protein
- I–J · 2026 Ų buried · 31 hydrogen bonds · protein-protein
- S–T · 2020 Ų buried · 31 hydrogen bonds · protein-protein
- M–N · 2018 Ų buried · 36 hydrogen bonds · protein-protein
Compared structures
- 1N8J · Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S) · the same entry in another collection · chain K against K, 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 P0A251
- Elsewhere: RCSB PDB 1N8J · PDBe 1N8J · UniProt P0A251
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