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Nitrilase-like protein NIT2 from kluyve-romyces lactis

Analyse Nitrilase-like protein NIT2 from kluyve-romyces lactis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ELF
Type: protein
Length: 1,169 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: KLLA0E15247P
UniProt: Q6CN52
Pockets: 8 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	KLLA0E15247P	protein	291	34% helix, 26% strand	Q6CN52
B	KLLA0E15247P	protein	293	34% helix, 27% strand	Q6CN52
C	KLLA0E15247P	protein	294	35% helix, 26% strand	Q6CN52

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	475	0.68	0.79	34	empty
2	463	0.67	0.79	33	empty
3	434	0.67	0.79	34	empty
4	429	0.66	0.78	31	empty
5	277	0.52	0.75	28	empty

Interfaces

4 interfaces between chains.

A–B · 461 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 153 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 115 Å² buried · 0 hydrogen bonds · protein-protein
C–D · 84 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7ELF · Nitrilase-Like Protein Nit2 from Kluyve-romyces lactis · 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 Q6CN52
Elsewhere: RCSB PDB 7ELF · PDBe 7ELF · UniProt Q6CN52

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