MolNFT v1 · #90626 · protein
Crystal structure of a disease-associated anti-human gm-csf autoantibody MB007
4EOW · MB007 human IGG1 Fab fragment heavy chain: “Crystal structure of a disease-associated anti-human gm-csf autoantibody MB007”. X-ray diffraction, 6 pockets (best druggability 0.50). MolNFT v1 #90626 on GenesisL1: 3D structure, binding…
- PDB
- 4EOW
- Type
- protein
- Length
- 439 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MB007 human IGG1 Fab fragment heavy chain; MB007 IGG1 Fab fragment light chain
- UniProt
- S6B291, P0DOY2
- Pockets
- 6 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | MB007 human IGG1 Fab fragment heavy chain | protein | 228 | 8% helix, 49% strand | S6B291 |
| L | MB007 IGG1 Fab fragment light chain | protein | 211 | 7% helix, 50% strand | P0DOY2 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.50 | 0.75 | 34 | empty |
| 2 | 116 | 0.50 | 0.80 | 18 | empty |
| 3 | 157 | 0.47 | 0.76 | 27 | empty |
| 4 | 130 | 0.40 | 0.75 | 27 | empty |
| 5 | 85 | 0.40 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- H–L · 1750 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4EOW · Crystal structure of a disease-associated anti-human GM-CSF autoantibody MB007 · the same entry in another collection · chain H against H, TM-score 1.00
- P0DOY2 · AlphaFold monomer V2.0 prediction for immunoglobulin lambda constant 2 (P0DOY2) · a predicted model of the same protein · chain L against A, TM-score 0.48
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 S6B291
- Every structure of UniProt P0DOY2
- Elsewhere: RCSB PDB 4EOW · PDBe 4EOW · UniProt S6B291 · UniProt P0DOY2
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