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Crystal structure of spire kind domain

Analyse Crystal structure of spire kind domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RBW
Type: protein
Length: 608 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein spire homolog 1
UniProt: Q08AE8
Pockets: 6 · best druggability 0.52

Structure

x-ray diffraction · 3 distinct chains · 55% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein spire homolog 1	protein	154	54% helix, 6% strand	Q08AE8
C	Protein spire homolog 1	protein	151	54% helix, 7% strand	Q08AE8
D	Protein spire homolog 1	protein	149	56% helix, 7% strand	Q08AE8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	239	0.52	0.76	30	empty
2	105	0.50	0.82	22	empty
3	71	0.49	0.84	17	empty
4	54	0.43	0.83	13	empty
5	53	0.38	0.80	12	empty

Interfaces

2 interfaces between chains.

B–D · 729 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 62 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3RBW · Crystal structure of Spire KIND domain · the same entry in another collection · chain A against A, TM-score 1.00
Q08AE8 · AlphaFold monomer V2.0 prediction for protein spire homolog 1 (Q08AE8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q08AE8
Elsewhere: RCSB PDB 3RBW · PDBe 3RBW · UniProt Q08AE8

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