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Crystal structure of de novo designed serine hydrolase OSH55.14_E3, northeast structural genomics consortium target OR342

Analyse Crystal structure of de novo designed serine hydrolase OSH55.14_E3, northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KYB
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Designed protein OR342
Ligands: PO4
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Designed protein OR342	protein	163	35% helix, 22% strand	—
B	Designed protein OR342	protein	155	40% helix, 24% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

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	56	0.57	0.90	19	empty
2	102	0.49	0.81	26	empty
3	111	0.44	0.78	29	empty
4	105	0.38	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 429 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

4KYB · Crystal Structure of de novo designed serine hydrolase OSH55.14_E3, Northeast Structural… · 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
Elsewhere: RCSB PDB 4KYB · PDBe 4KYB

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