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Complex SECA:ADP from escherichia COLI

Analyse Complex SECA:ADP from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FSI
Type: protein
Length: 1,439 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Preprotein translocase seca subunit
UniProt: P10408
Ligands: ADP
Pockets: 16 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 57% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Preprotein translocase seca subunit	protein	691	58% helix, 11% strand	P10408
B	Preprotein translocase seca subunit	protein	748	55% helix, 10% strand	P10408

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1192	0.78	0.80	130	ADP
2	696	0.74	0.80	71	empty
3	484	0.65	0.78	60	empty
4	282	0.64	0.81	42	empty
5	213	0.61	0.82	24	empty

Interfaces

1 interface between chains.

A–B · 1432 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

2FSI · Complex SecA:ADP from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P10408 · AlphaFold monomer V2.0 prediction for protein translocase subunit seca (P10408) · a predicted model of the same protein · chain A against A, TM-score 0.90

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10408
Elsewhere: RCSB PDB 2FSI · PDBe 2FSI · UniProt P10408

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