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Crystal structure of haemophilus influenzae oppa complex with rppgfspfr

Analyse Crystal structure of haemophilus influenzae oppa complex with rppgfspfr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DTH
Type: protein
Length: 518 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Periplasmic oligopeptide-binding protein; Arg-pro-pro-gly-phe
UniProt: Q4QLH0
Ligands: SO4
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Periplasmic oligopeptide-binding protein	protein	513	35% helix, 22% strand	Q4QLH0
B	Arg-pro-pro-gly-phe	protein	5	0% helix, 0% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.51	0.83	21	empty
2	91	0.38	0.76	20	empty
3	70	0.37	0.78	23	empty

Interfaces

1 interface between chains.

A–B · 600 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6DTH · Crystal structure of Haemophilus influenzae OppA complex with RPPGFSPFR · 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 Q4QLH0
Elsewhere: RCSB PDB 6DTH · PDBe 6DTH · UniProt Q4QLH0

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