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Dark-state structure of appa wild-type without the cys-rich region from rb. sphaeroides

Analyse Dark-state structure of appa wild-type without the cys-rich region from rb.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HH1
Type: protein
Length: 765 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Appa protein
UniProt: Q53119
Ligands: FMN
Pockets: 13 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Appa protein	protein	383	52% helix, 17% strand	Q53119
B	Appa protein	protein	382	52% helix, 16% strand	Q53119

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	647	0.79	0.84	64	empty
2	655	0.77	0.82	80	empty
3	105	0.65	0.89	22	empty
4	196	0.61	0.83	26	empty
5	136	0.61	0.85	19	FMN

Interfaces

1 interface between chains.

A–B · 1175 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4HH1 · Dark-state structure of AppA wild-type without the Cys-rich region from Rb. sphaeroides · 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 Q53119
Elsewhere: RCSB PDB 4HH1 · PDBe 4HH1 · UniProt Q53119

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