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Crystal structure of BA3275, the member of S66 family of serine peptidases

Analyse Crystal structure of BA3275, the member of S66 family of serine peptidases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5F1Y
Type: protein
Length: 686 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mccc family protein
UniProt: Q734X3
Pockets: 6 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Mccc family protein	protein	343	36% helix, 21% strand	Q734X3

Ligands and binding sites

GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	333	0.69	0.82	40	GOL
2	368	0.67	0.80	51	empty
3	57	0.47	0.85	15	empty
4	71	0.46	0.83	21	empty
5	50	0.43	0.84	16	empty

Interfaces

1 interface between chains.

A–B · 1210 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 modified (engineered).

Compared structures

5F1Y · Crystal structure of Ba3275, the member of S66 family of serine peptidases · 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 Q734X3
Elsewhere: RCSB PDB 5F1Y · PDBe 5F1Y · UniProt Q734X3

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