Research workbench

Salmonella export gate and rod refined in focussed C1 MAP

Analyse Salmonella export gate and rod refined in focussed C1 MAP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BIN
Type: protein
Length: 10,887 residues
Chains: 56
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flagellar biosynthetic protein flip; Flagellar biosynthetic protein flir; Flagellar…
UniProt: Q8Z5R3, A0A3U0BCQ2, A0A3Y0WXN7, P26462, P16437, P0A1I7, P16323, P0A1J3
Pockets: 20 · best druggability 0.91

Structure

electron microscopy · 16 distinct chains · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Flagellar biosynthetic protein flip	protein	209	71% helix, 0% strand	Q8Z5R3
F	Flagellar biosynthetic protein flir	protein	258	67% helix, 0% strand	A0A3U0BCQ2
G, H, I, J	Flagellar biosynthetic protein fliq	protein	89	75% helix, 0% strand	A0A3Y0WXN7
K	Flagellar hook-basal body complex protein flie	protein	39	85% helix, 0% strand	P26462
L, M, N, O, P	Flagellar hook-basal body complex protein flie	protein	75	80% helix, 0% strand	P26462
Q	Flagellar basal body rod protein flgb	protein	133	49% helix, 5% strand	P16437
R	Flagellar basal body rod protein flgb	protein	120	53% helix, 3% strand	P16437
S	Flagellar basal body rod protein flgb	protein	122	55% helix, 3% strand	P16437
T	Flagellar basal body rod protein flgb	protein	106	61% helix, 4% strand	P16437
U	Flagellar basal body rod protein flgb	protein	119	54% helix, 3% strand	P16437
V	Flagellar basal-body rod protein flgc	protein	133	44% helix, 9% strand	P0A1I7
W, X, Y, Z, a	Flagellar basal-body rod protein flgc	protein	132	44% helix, 8% strand	P0A1I7
b, c, d, e, f	Flagellar basal-body rod protein flgf	protein	249	25% helix, 25% strand	P16323
g, h, i, j, k, r, s, t, u, v, w, x, y, z, 1, 2, 3, 4	Flagellar basal-body rod protein flgg	protein	260	24% helix, 29% strand	P0A1J3
l, m, n, o, p	Flagellar basal-body rod protein flgg	protein	249	23% helix, 29% strand	P0A1J3
q	Flagellar basal-body rod protein flgg	protein	251	24% helix, 30% strand	P0A1J3

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	873	0.91	0.94	126	empty
2	1179	0.90	0.92	152	empty
3	1176	0.89	0.91	150	empty
4	1052	0.89	0.90	119	empty
5	1136	0.89	0.90	112	empty

Interfaces

244 interfaces between chains.

y–4 · 2788 Å² buried · 25 hydrogen bonds · protein-protein
q–v · 2755 Å² buried · 33 hydrogen bonds · protein-protein
m–r · 2732 Å² buried · 36 hydrogen bonds · protein-protein
n–t · 2726 Å² buried · 30 hydrogen bonds · protein-protein
s–x · 2716 Å² buried · 31 hydrogen bonds · protein-protein

Compared structures

7BIN · Salmonella export gate and rod refined in focussed C1 map · 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 Q8Z5R3
Every structure of UniProt A0A3U0BCQ2
Every structure of UniProt A0A3Y0WXN7
Every structure of UniProt P26462
Every structure of UniProt P16437
Every structure of UniProt P0A1I7
Every structure of UniProt P16323
Every structure of UniProt P0A1J3
Elsewhere: RCSB PDB 7BIN · PDBe 7BIN · UniProt Q8Z5R3 · UniProt A0A3U0BCQ2 · UniProt A0A3Y0WXN7 · UniProt P26462 · UniProt P16437 · UniProt P0A1I7 · UniProt P16323 · UniProt P0A1J3

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