MolNFT v1 · #27303 · protein
Crystal structure of the CDR2 germline reversion mutant of cab-LYS3 in complex with hen egg white lysozyme
1XFP · Heavy chain antibody: “Crystal structure of the CDR2 germline reversion mutant of cab-LYS3 in complex with hen egg white lysozyme”. X-ray diffraction, 2 pockets (best druggability 0.34). MolNFT v1 #27303 on GenesisL1: 3D structure…
- PDB
- 1XFP
- Type
- protein
- Length
- 260 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heavy chain antibody; Lysozyme C
- EC
- 3.2.1.17
- UniProt
- P00698
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heavy chain antibody | protein | 131 | 8% helix, 47% strand | — |
| L | Lysozyme C (EC 3.2.1.17) | protein | 129 | 41% helix, 11% strand | P00698 |
Ligands and binding sites
- FMT · Formic acid · additive · 8 copies · chains A, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.34 | 0.77 | 18 | empty |
| 2 | 55 | 0.25 | 0.72 | 16 | FMT |
Interfaces
1 interface between chains.
- A–L · 741 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1XFP · Crystal structure of the CDR2 germline reversion mutant of cAb-Lys3 in complex with hen… · 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 P00698
- Elsewhere: RCSB PDB 1XFP · PDBe 1XFP · UniProt P00698
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