MolNFT v1 · #188517 · protein
Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation
7TW0: “Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation”. Electron microscopy, 1 ligand (NAG). MolNFT v1 #188517 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7TW0
- Type
- protein
- Length
- 2,309 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02730, P16452
- Ligands
- NAG
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 814 | — | P02730 |
| A | — | protein | 830 | — | P02730 |
| E | — | protein | 665 | — | P16452 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7TW0 · Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation · the same entry in another collection · chain B against B, TM-score 1.00
- P16452 · AlphaFold monomer V2.0 prediction for protein 4.2 (P16452) · a predicted model of the same protein · chain E against A, TM-score 0.96
- P02730 · AlphaFold monomer V2.0 prediction for band 3 anion transport protein (P02730) · a predicted model of the same protein · chain B against A, TM-score 0.65
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 P02730
- Every structure of UniProt P16452
- Elsewhere: RCSB PDB 7TW0 · PDBe 7TW0 · UniProt P02730 · UniProt P16452
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