MolNFT v1 · #40305 · protein
Crystal structure of the hypothetical lipoprotein ymcc from escherichia COLI (K12), northeast structural genomics target ER552.
2IN5: “Crystal structure of the hypothetical lipoprotein ymcc from escherichia COLI (K12), northeast structural…”. X-ray diffraction, 5 pockets (best druggability 0.45). MolNFT v1 #40305 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2IN5
- Type
- protein
- Length
- 383 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical lipoprotein ymcc
- UniProt
- P75884
- Pockets
- 5 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical lipoprotein ymcc | protein | 195 | 14% helix, 53% strand | P75884 |
| B | Hypothetical lipoprotein ymcc | protein | 188 | 10% helix, 57% strand | P75884 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.45 | 0.81 | 20 | empty |
| 2 | 123 | 0.42 | 0.76 | 23 | empty |
| 3 | 94 | 0.41 | 0.77 | 16 | empty |
| 4 | 70 | 0.32 | 0.75 | 18 | empty |
| 5 | 57 | 0.29 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1324 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2IN5 · Crystal Structure of the hypothetical lipoprotein YmcC from Escherichia coli (K12)… · the same entry in another collection · chain A against A, TM-score 1.00
- P75884 · AlphaFold monomer V2.0 prediction for uncharacterized lipoprotein gfcb (P75884) · a predicted model of the same protein · chain A 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 P75884
- Elsewhere: RCSB PDB 2IN5 · PDBe 2IN5 · UniProt P75884
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