MolNFT v1 · #31687 · protein

Structure of MAR1 ribonuclease from caenorhabditis elegans

2B34: “Structure of MAR1 ribonuclease from caenorhabditis elegans”. X-ray diffraction, 20 pockets (best druggability 0.84). MolNFT v1 #31687 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2B34
Type: protein
Length: 1,536 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAR1 ribonuclease
UniProt: Q20062
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	MAR1 ribonuclease	protein	192	41% helix, 21% strand	Q20062

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	640	0.84	0.88	71	empty
2	706	0.82	0.86	76	empty
3	281	0.68	0.83	27	empty
4	639	0.66	0.76	73	empty
5	284	0.65	0.81	24	empty

Interfaces

15 interfaces between chains.

C–D · 1411 Å² buried · 22 hydrogen bonds · protein-protein
B–C · 1386 Å² buried · 26 hydrogen bonds · protein-protein
A–D · 1373 Å² buried · 24 hydrogen bonds · protein-protein
E–F · 1368 Å² buried · 24 hydrogen bonds · protein-protein
E–H · 1357 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2B34 · Structure of MAR1 Ribonuclease from Caenorhabditis elegans · 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 Q20062
Elsewhere: RCSB PDB 2B34 · PDBe 2B34 · UniProt Q20062

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