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Crystal structure of protein APE2225 from aeropyrum pernix K1, pfam coxg

Analyse Crystal structure of protein APE2225 from aeropyrum pernix K1, pfam coxg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NS9
Type: protein
Length: 304 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein APE2225
UniProt: Q9Y9R3
Ligands: PO4
Pockets: 2 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein APE2225	protein	152	28% helix, 54% strand	Q9Y9R3
B	Hypothetical protein APE2225	protein	152	27% helix, 55% strand	Q9Y9R3

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	613	0.88	0.92	51	PO4
2	601	0.88	0.92	49	PO4

Interfaces

1 interface between chains.

A–B · 1066 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

2NS9 · Crystal structure of protein APE2225 from Aeropyrum pernix K1, Pfam COXG · 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 Q9Y9R3
Elsewhere: RCSB PDB 2NS9 · PDBe 2NS9 · UniProt Q9Y9R3

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