MolNFT v1 · #162033 · protein + RNA

Influenza B virus (B/PANAMA/45) polymerase hetermotrimer in complex with 3'5' crna promoter

6QWL · Polymerase acidic protein: “Influenza B virus (B/PANAMA/45) polymerase hetermotrimer in complex with 3'5' crna promoter”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #162033 on GenesisL1: 3D structure…

PDB: 6QWL
Type: protein + RNA
Length: 1,270 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase acidic protein; RNA-directed RNA polymerase catalytic subunit; Polymerase…
EC: 3.1.-.-, 2.7.7.48
UniProt: O36432, O36430, O36431
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 5 distinct chains · 42% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Polymerase acidic protein (EC 3.1.-.-)	protein	511	42% helix, 12% strand	O36432
K	RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48)	protein	539	42% helix, 11% strand	O36430
Q	Polymerase basic protein 2	protein	194	40% helix, 16% strand	O36431
T	3' crna	rna	12	—	—
W	5' crna	rna	14	—	—

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	324	0.78	0.89	45	empty
2	110	0.75	0.95	23	empty
3	583	0.74	0.81	66	empty
4	470	0.72	0.82	48	empty
5	366	0.69	0.82	49	empty

Interfaces

8 interfaces between chains.

E–K · 6176 Å² buried · 84 hydrogen bonds · protein-protein
K–Q · 2356 Å² buried · 19 hydrogen bonds · protein-protein
E–W · 1140 Å² buried · 21 hydrogen bonds · protein-nucleic
E–T · 707 Å² buried · 10 hydrogen bonds · protein-nucleic
K–T · 376 Å² buried · 5 hydrogen bonds · protein-nucleic

Compared structures

6QWL · Influenza B virus (B/Panama/45) polymerase Hetermotrimer in complex with 3'5' cRNA… · the same entry in another collection · chain E against E, 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 O36432
Every structure of UniProt O36430
Every structure of UniProt O36431
Elsewhere: RCSB PDB 6QWL · PDBe 6QWL · UniProt O36432 · UniProt O36430 · UniProt O36431

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