MolNFT v1 · #31232 · protein

Structural genomics, the crystal structure of a phage protein (PHBC6A51) from bacillus cereus atcc 14579

2AO9: “Structural genomics, the crystal structure of a phage protein (PHBC6A51) from bacillus cereus atcc 14579”. X-ray diffraction, 19 pockets (best druggability 0.63). MolNFT v1 #31232 on GenesisL1: 3D structure, binding sites and…

PDB: 2AO9
Type: protein
Length: 999 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phage protein
UniProt: Q81ES4
Pockets: 19 · best druggability 0.63

Structure

x-ray diffraction · 9 distinct chains · 68% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phage protein	protein	117	68% helix, 7% strand	Q81ES4
B	Phage protein	protein	114	69% helix, 6% strand	Q81ES4
C	Phage protein	protein	117	68% helix, 8% strand	Q81ES4
D	Phage protein	protein	107	67% helix, 7% strand	Q81ES4
E	Phage protein	protein	115	69% helix, 7% strand	Q81ES4
F	Phage protein	protein	110	72% helix, 7% strand	Q81ES4
G	Phage protein	protein	106	68% helix, 7% strand	Q81ES4
H	Phage protein	protein	114	64% helix, 6% strand	Q81ES4
I	Phage protein	protein	99	63% helix, 8% strand	Q81ES4

Pockets

19 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	538	0.63	0.74	31	empty
2	326	0.60	0.78	39	empty
3	156	0.59	0.83	28	empty
4	229	0.52	0.76	32	empty
5	237	0.50	0.75	28	empty

Interfaces

18 interfaces between chains.

C–D · 2172 Å² buried · 34 hydrogen bonds · protein-protein
A–G · 2139 Å² buried · 35 hydrogen bonds · protein-protein
B–D · 2106 Å² buried · 37 hydrogen bonds · protein-protein
B–E · 2077 Å² buried · 35 hydrogen bonds · protein-protein
F–G · 2047 Å² buried · 33 hydrogen bonds · protein-protein

Compared structures

2AO9 · Structural Genomics, The crystal structure of a Phage protein (phBC6A51) from Bacillus… · 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 Q81ES4
Elsewhere: RCSB PDB 2AO9 · PDBe 2AO9 · UniProt Q81ES4

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