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A V49A mutation induces 3D domain swapping in the B1 domain of protein L from peptostreptococcus magnus

Analyse A V49A mutation induces 3D domain swapping in the B1 domain of protein L from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1K50
Type: protein
Length: 252 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein L
UniProt: Q51912
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Protein L	protein	63	33% helix, 44% strand	Q51912

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	100	0.43	0.78	23	empty
2	95	0.38	0.76	18	empty

Interfaces

6 interfaces between chains.

B–D · 2082 Å² buried · 49 hydrogen bonds · protein-protein
A–B · 721 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 598 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 367 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 169 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1K50 · A V49A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from… · 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 Q51912
Elsewhere: RCSB PDB 1K50 · PDBe 1K50 · UniProt Q51912

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