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F1FO-ATP synthase from acinetobacter baumannii (state 1)

Analyse F1FO-ATP synthase from acinetobacter baumannii (state 1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P2Y
Type: protein
Length: 4,904 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, PO4
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	509	42% helix, 18% strand	A3M142
B	ATP synthase subunit alpha (EC 7.1.2.2)	protein	514	42% helix, 18% strand	A3M142
C	ATP synthase subunit alpha (EC 7.1.2.2)	protein	509	42% helix, 18% strand	A3M142
D, E	ATP synthase subunit beta (EC 7.1.2.2)	protein	463	37% helix, 19% strand	A3M144
F	ATP synthase subunit beta (EC 7.1.2.2)	protein	464	37% helix, 20% strand	A3M144
G, H, P, Q	ATP synthase subunit C	protein	79	90% helix, 0% strand	A3M139
J, K, L, O, R, S	ATP synthase subunit C	protein	80	90% helix, 0% strand	A3M139
a	ATP synthase subunit a	protein	277	68% helix, 0% strand	A3M137
b	ATP synthase subunit B	protein	154	84% helix, 0% strand	A3M140
d	ATP synthase subunit delta	protein	174	61% helix, 12% strand	A3M141
e	ATP synthase epsilon chain	protein	138	28% helix, 38% strand	A3M145
g	ATP synthase gamma chain	protein	288	60% helix, 13% strand	A3M143
p	ATP synthase subunit B	protein	155	96% 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 A, D
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
PO4 · Phosphate ion · ion · chains 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	1142	0.89	0.90	147	ATP, MG
2	1001	0.88	0.89	124	ATP, MG
3	552	0.84	0.90	71	MG, ATP
4	594	0.82	0.88	84	empty
5	324	0.82	0.92	40	empty

Interfaces

61 interfaces between chains.

A–D · 2889 Å² buried · 28 hydrogen bonds · protein-protein
C–D · 2416 Å² buried · 17 hydrogen bonds · protein-protein
C–E · 2374 Å² buried · 21 hydrogen bonds · protein-protein
e–g · 2312 Å² buried · 12 hydrogen bonds · protein-protein
b–p · 2172 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7P2Y · F1Fo-ATP synthase from Acinetobacter baumannii (state 1) · the same entry in another collection · chain C against C, 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 7P2Y · PDBe 7P2Y · UniProt A3M142 · UniProt A3M144 · UniProt A3M139 · UniProt A3M137 · UniProt A3M140 · UniProt A3M141 · UniProt A3M145 · UniProt A3M143

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