MolNFT v1 · #159886 · protein
HYHEL10 Fab complexed with hen egg lysozyme carrying two mutations (HEL2X-rigid): R21Q and R73E
6P4A · HYHEL10 Fab light chain: “HYHEL10 Fab complexed with hen egg lysozyme carrying two mutations (HEL2X-rigid): R21Q and R73E”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #159886 on GenesisL1: 3D structure, binding…
- PDB
- 6P4A
- Type
- protein
- Length
- 552 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HYHEL10 Fab light chain; HYHEL10 Fab heavy chain; Lysozyme C
- EC
- 3.2.1.17
- UniProt
- A0A0E4B213, P00698
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | HYHEL10 Fab light chain | protein | 214 | 6% helix, 51% strand | A0A0E4B213 |
| H | HYHEL10 Fab heavy chain | protein | 209 | 7% helix, 53% strand | — |
| C | Lysozyme C (EC 3.2.1.17) | protein | 129 | 41% helix, 11% strand | P00698 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.65 | 0.87 | 30 | empty |
| 2 | 393 | 0.56 | 0.74 | 43 | empty |
| 3 | 105 | 0.38 | 0.75 | 24 | empty |
| 4 | 77 | 0.35 | 0.76 | 17 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1952 Ų buried · 14 hydrogen bonds · protein-protein
- H–C · 615 Ų buried · 17 hydrogen bonds · protein-protein
- L–C · 348 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 6P4A · HyHEL10 Fab complexed with hen egg lysozyme carrying two mutations (HEL2x-rigid): R21Q… · the same entry in another collection · chain L against L, 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 A0A0E4B213
- Every structure of UniProt P00698
- Elsewhere: RCSB PDB 6P4A · PDBe 6P4A · UniProt A0A0E4B213 · UniProt P00698
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