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Structure of shwanavidin low affinity mutant (F43A)

Analyse Structure of shwanavidin low affinity mutant (F43A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3T2X
Type: protein
Length: 474 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AVIDIN/STREPTAVIDIN
UniProt: Q12QS6
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	AVIDIN/STREPTAVIDIN	protein	119	3% helix, 62% strand	Q12QS6
C	AVIDIN/STREPTAVIDIN	protein	117	3% helix, 62% strand	Q12QS6

Pockets

3 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	902	0.74	0.78	77	empty
2	125	0.44	0.76	18	empty
3	103	0.42	0.77	19	empty

Interfaces

3 interfaces between chains.

A–B · 1727 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 1712 Å² buried · 26 hydrogen bonds · protein-protein
A–C · 399 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3T2X · Structure of shwanavidin low affinity mutant (F43A) · the same entry in another collection · chain B against B, 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 Q12QS6
Elsewhere: RCSB PDB 3T2X · PDBe 3T2X · UniProt Q12QS6

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