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ABC transporter-associated periplasmic binding protein dppa from helicobacter pylori in complex with peptide stsa

Analyse ABC transporter-associated periplasmic binding protein dppa from helicobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OFQ
Type: protein
Length: 516 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme-binding protein a / ai-2 binding protein a; Ser-thr-ser-ala
UniProt: A0A1U9ISL1
Pockets: 5 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme-binding protein a / ai-2 binding protein a	protein	512	34% helix, 23% strand	A0A1U9ISL1
B	Ser-thr-ser-ala	protein	4	0% helix, 25% strand	—

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	584	0.86	0.92	68	empty
2	111	0.77	0.96	25	empty
3	56	0.59	0.91	23	empty
4	237	0.50	0.75	34	empty
5	78	0.32	0.74	27	empty

Interfaces

1 interface between chains.

A–B · 376 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6OFQ · ABC transporter-associated periplasmic binding protein DppA from Helicobacter pylori in… · 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 A0A1U9ISL1
Elsewhere: RCSB PDB 6OFQ · PDBe 6OFQ · UniProt A0A1U9ISL1

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