MolNFT v1 · #127925 · protein
Crystal structures of homooligomers of collagen type IV. ALPHA2NC1
5NB2 · Collagen alpha-2(IV) chain: “Crystal structures of homooligomers of collagen type IV. ALPHA2NC1”. X-ray diffraction, 3 pockets (best druggability 0.49). MolNFT v1 #127925 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NB2
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Collagen alpha-2(IV) chain
- UniProt
- P08572
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Collagen alpha-2(IV) chain | protein | 191 | 8% helix, 40% strand | P08572 |
| B | Collagen alpha-2(IV) chain | protein | 170 | 9% helix, 43% strand | P08572 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.49 | 0.76 | 29 | empty |
| 2 | 83 | 0.37 | 0.76 | 18 | empty |
| 3 | 63 | 0.35 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 354 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 5NB2 · Crystal structures of homooligomers of collagen type IV. alpha2NC1 · the same entry in another collection · chain A against A, TM-score 1.00
- P08572 · AlphaFold monomer V2.0 prediction for collagen alpha-2(IV) chain (P08572) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P08572
- Elsewhere: RCSB PDB 5NB2 · PDBe 5NB2 · UniProt P08572
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