Research workbench

F1FO-ATP synthase from acinetobacter baumannii (state 2)

Analyse F1FO-ATP synthase from acinetobacter baumannii (state 2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P3N
Type: protein
Length: 4,895 residues
Chains: 22
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP synthase subunit alpha; ATP synthase subunit beta; ATP synthase subunit C; ATP…
EC: 7.1.2.2
UniProt: A3M142, A3M144, A3M139, A3M137, A3M140, A3M141, A3M145, A3M143
Ligands: ATP, ADP, MG
Pockets: 20 · best druggability 0.89

Structure

electron microscopy · 13 distinct chains · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP synthase subunit alpha (EC 7.1.2.2)	protein	512	43% helix, 20% strand	A3M142
B	ATP synthase subunit alpha (EC 7.1.2.2)	protein	514	40% helix, 18% strand	A3M142
C	ATP synthase subunit alpha (EC 7.1.2.2)	protein	506	42% helix, 19% strand	A3M142
D	ATP synthase subunit beta (EC 7.1.2.2)	protein	464	39% helix, 20% strand	A3M144
E, F	ATP synthase subunit beta (EC 7.1.2.2)	protein	463	38% helix, 17% strand	A3M144
G, K, L, S	ATP synthase subunit C	protein	79	86% helix, 0% strand	A3M139
H, J, O, P, Q, R	ATP synthase subunit C	protein	80	90% helix, 0% strand	A3M139
a	ATP synthase subunit a	protein	277	65% helix, 0% strand	A3M137
b	ATP synthase subunit B	protein	145	85% helix, 0% strand	A3M140
d	ATP synthase subunit delta	protein	174	59% helix, 9% strand	A3M141
e	ATP synthase epsilon chain	protein	138	30% helix, 41% strand	A3M145
g	ATP synthase gamma chain	protein	288	59% helix, 14% strand	A3M143
p	ATP synthase subunit B	protein	155	97% helix, 0% strand	A3M140

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 3 copies · chains A, F, B, E, C, D
ADP · Adenosine-5'-diphosphate · ligand · chains C, E
MG · Magnesium ion · metal · 4 copies · chains A, B, C, E

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1007	0.89	0.90	133	empty
2	845	0.87	0.89	99	empty
3	1073	0.86	0.87	116	empty
4	1001	0.86	0.87	128	empty
5	662	0.86	0.90	89	empty

Interfaces

58 interfaces between chains.

C–E · 2529 Å² buried · 28 hydrogen bonds · protein-protein
B–F · 2254 Å² buried · 19 hydrogen bonds · protein-protein
B–E · 2159 Å² buried · 22 hydrogen bonds · protein-protein
e–g · 2117 Å² buried · 30 hydrogen bonds · protein-protein
A–F · 1787 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

7P3N · F1Fo-ATP synthase from Acinetobacter baumannii (state 2) · the same entry in another collection · chain J against J, 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 A3M142
Every structure of UniProt A3M144
Every structure of UniProt A3M139
Every structure of UniProt A3M137
Every structure of UniProt A3M140
Every structure of UniProt A3M141
Every structure of UniProt A3M145
Every structure of UniProt A3M143
Elsewhere: RCSB PDB 7P3N · PDBe 7P3N · UniProt A3M142 · UniProt A3M144 · UniProt A3M139 · UniProt A3M137 · UniProt A3M140 · UniProt A3M141 · UniProt A3M145 · UniProt A3M143

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