Research workbench
Human Fab 5H2 bound to nhba-C3 from neisseria meningitidis serogroup B
Analyse Human Fab 5H2 bound to nhba-C3 from neisseria meningitidis serogroup B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O1R
- Type
- protein
- Length
- 1,100 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9JPP1, Q6GMX6, Q6GMX0
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 115 | — | Q9JPP1 |
| B | — | protein | 115 | — | Q9JPP1 |
| H | — | protein | 226 | — | Q6GMX6 |
| I | — | protein | 221 | — | Q6GMX6 |
| L | — | protein | 211 | — | Q6GMX0 |
| M | — | protein | 212 | — | Q6GMX0 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, H, I, M, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5O1R · human Fab 5H2 bound to NHBA-C3 from Neisseria meningitidis serogroup B · the same entry in another collection · chain H against H, 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 Q9JPP1
- Every structure of UniProt Q6GMX6
- Every structure of UniProt Q6GMX0
- Elsewhere: RCSB PDB 5O1R · PDBe 5O1R · UniProt Q9JPP1 · UniProt Q6GMX6 · UniProt Q6GMX0
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