MolNFT v1 · #127854 · protein

Enah EVH1 in complex with ac-[2-cl-F]-pppp-oh

5N91 · Protein enabled homolog: “Enah EVH1 in complex with ac-[2-cl-F]-pppp-oh”. X-ray diffraction, 3 ligands (ACE, 2L5, NO3), 1 pocket (best druggability 0.60). MolNFT v1 #127854 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5N91
Type: protein
Length: 235 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein enabled homolog; Ac-[2-cl-F]-pppp-oh
UniProt: Q8N8S7
Ligands: ACE, 2L5, NO3
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 3 distinct chains · 18% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein enabled homolog	protein	113	18% helix, 47% strand	Q8N8S7
B	Protein enabled homolog	protein	110	18% helix, 51% strand	Q8N8S7
E, F, G	Ac-[2-cl-F]-pppp-oh	protein	4	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 3 copies · chains B, E, A, F, G
2L5 · 2-chloro-L-phenylalanine · ligand · 3 copies · chains B, E, A, F, G
NO3 · Nitrate ion · ion · 4 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	360	0.60	0.77	36	empty

Interfaces

4 interfaces between chains.

A–B · 567 Å² buried · 10 hydrogen bonds · protein-protein
A–F · 232 Å² buried · 3 hydrogen bonds · protein-protein
B–E · 232 Å² buried · 3 hydrogen bonds · protein-protein
A–G · 197 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

5N91 · ENAH EVH1 in complex with Ac-[2-Cl-F]-PPPP-OH · the same entry in another collection · chain B against B, TM-score 1.00
Q8N8S7 · AlphaFold monomer V2.0 prediction for protein enabled homolog (Q8N8S7) · a predicted model of the same protein · chain B 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 Q8N8S7
Elsewhere: RCSB PDB 5N91 · PDBe 5N91 · UniProt Q8N8S7

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