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Crystal structure of a bifunctional protein (csaa) with export-related chaperone and tRNA-binding activities.

Analyse Crystal structure of a bifunctional protein (csaa) with export-related… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GD7
Type: protein
Length: 436 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Csaa protein
UniProt: Q9AQH8
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Csaa protein	protein	109	13% helix, 42% strand	Q9AQH8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	240	0.55	0.77	26	empty
2	138	0.45	0.77	24	empty
3	108	0.41	0.76	23	empty
4	88	0.40	0.77	19	empty

Interfaces

5 interfaces between chains.

A–B · 1671 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 1638 Å² buried · 20 hydrogen bonds · protein-protein
B–C · 218 Å² buried · 1 hydrogen bond · protein-protein
B–D · 148 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 113 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1GD7 · Crystal structure of a bifunctional protein (csaa) with export-related chaperone and… · 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 Q9AQH8
Elsewhere: RCSB PDB 1GD7 · PDBe 1GD7 · UniProt Q9AQH8

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