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Structure of the la crosse bunyavirus polymerase in complex with the 3' viral RNA

Analyse Structure of the la crosse bunyavirus polymerase in complex with the 3' viral… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AMR
Type: protein + RNA
Length: 1,681 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA polymerase L; RNA
EC: 2.7.7.48
UniProt: A5HC98
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 54% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA polymerase L (EC 2.7.7.48)	protein	1657	54% helix, 12% strand	A5HC98
B	RNA	rna	16	—	—
C	RNA	rna	8	—	—

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	402	0.78	0.87	33	empty
2	490	0.78	0.85	42	empty
3	440	0.69	0.80	43	empty
4	314	0.68	0.82	27	empty
5	501	0.65	0.77	58	empty

Interfaces

3 interfaces between chains.

A–B · 1731 Å² buried · 48 hydrogen bonds · protein-nucleic
B–C · 375 Å² buried · 31 hydrogen bonds · nucleic-nucleic
A–C · 206 Å² buried · 4 hydrogen bonds · protein-nucleic

Compared structures

5AMR · Structure of the La Crosse Bunyavirus polymerase in complex with the 3' viral RNA · 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 A5HC98
Elsewhere: RCSB PDB 5AMR · PDBe 5AMR · UniProt A5HC98

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