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NICA2 with cofactor FAD

Analyse NICA2 with cofactor FAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C4A
Type: protein
Length: 871 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amine oxidase
UniProt: F8G0P2
Ligands: FAD
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amine oxidase	protein	435	36% helix, 25% strand	F8G0P2
B	Amine oxidase	protein	436	36% helix, 24% strand	F8G0P2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

5 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	1160	0.86	0.86	105	FAD
2	1133	0.86	0.86	109	FAD
3	166	0.60	0.83	34	empty
4	170	0.53	0.79	28	empty
5	192	0.52	0.78	28	empty

Interfaces

1 interface between chains.

A–B · 1669 Å² buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

7C4A · nicA2 with cofactor FAD · 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 F8G0P2
Elsewhere: RCSB PDB 7C4A · PDBe 7C4A · UniProt F8G0P2

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