MolNFT v1 · #92559 · protein
Crystal structure of an immune complex at pH 6.5
4GBX: “Crystal structure of an immune complex at pH 6.5”. X-ray diffraction. MolNFT v1 #92559 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4GBX
- Type
- protein
- Length
- 759 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28067, P28068, P01903, P04229
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 189 | — | P28067 |
| D | — | protein | 191 | — | P28068 |
| A | — | protein | 180 | — | P01903 |
| B | — | protein | 189 | — | P04229 |
| E | — | protein | 10 | — | — |
Compared structures
- 4GBX · Crystal structure of an immune complex at pH 6.5 · the same entry in another collection · chain E against E, TM-score 1.00
- P28067 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dm alpha… · a predicted model of the same protein · chain C against A, TM-score 0.98
- P28068 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dm beta… · a predicted model of the same protein · chain D against A, TM-score 0.93
- P01903 · AlphaFold monomer V2.0 prediction for HLA class II histocompatibility antigen, dr alpha… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P28067
- Every structure of UniProt P28068
- Every structure of UniProt P01903
- Every structure of UniProt P04229
- Elsewhere: RCSB PDB 4GBX · PDBe 4GBX · UniProt P28067 · UniProt P28068 · UniProt P01903 · UniProt P04229
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.