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Crystal structure of ribosome-associated protein Y (psrp-1) from clostridium acetobutylicum. northeast structural genomics consortium target id CAR123A

Analyse Crystal structure of ribosome-associated protein Y (psrp-1) from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KA5
Type: protein
Length: 116 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribosome-associated protein Y (psrp-1)
UniProt: Q97F93
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribosome-associated protein Y (psrp-1)	protein	57	19% helix, 42% strand	Q97F93
B	Ribosome-associated protein Y (psrp-1)	protein	59	19% helix, 41% strand	Q97F93

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.42	0.76	17	empty
2	113	0.42	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 1242 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3KA5 · Crystal structure of Ribosome-associated protein Y (PSrp-1) from Clostridium… · 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 Q97F93
Elsewhere: RCSB PDB 3KA5 · PDBe 3KA5 · UniProt Q97F93

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