Research workbench
Bartonella henselae nrnc complexed with paaagg in the presence of CA2+. D4 symmetry.
Analyse Bartonella henselae nrnc complexed with paaagg in the presence of CA2+. D4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MQH
- Type
- protein + RNA
- Length
- 1,656 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nanornase C; RNA (5'-R(P*AP*AP*AP*GP*G)-3')
- UniProt
- X5MEI1
- Pockets
- 20 · best druggability 0.63
Structure
electron microscopy · 2 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O | Nanornase C | protein | 205 | 40% helix, 16% strand | X5MEI1 |
| B, D, F, H, J, L, N, P | RNA (5'-R(P*AP*AP*AP*GP*G)-3') | rna | 2 | — | — |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 433 | 0.63 | 0.77 | 48 | empty |
| 2 | 450 | 0.63 | 0.77 | 48 | empty |
| 3 | 412 | 0.62 | 0.77 | 48 | empty |
| 4 | 428 | 0.61 | 0.76 | 44 | empty |
| 5 | 263 | 0.59 | 0.79 | 32 | empty |
Interfaces
40 interfaces between chains.
- G–O · 1247 Ų buried · 5 hydrogen bonds · protein-protein
- A–M · 1242 Ų buried · 5 hydrogen bonds · protein-protein
- E–I · 1241 Ų buried · 5 hydrogen bonds · protein-protein
- C–K · 1232 Ų buried · 5 hydrogen bonds · protein-protein
- A–G · 412 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7MQH · Bartonella henselae NrnC complexed with pAAAGG in the presence of Ca2+. D4 Symmetry. · the same entry in another collection · chain A against A, 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 X5MEI1
- Elsewhere: RCSB PDB 7MQH · PDBe 7MQH · UniProt X5MEI1
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