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Structure of dpp III from bacteroides thetaiotaomicron

Analyse Structure of dpp III from bacteroides thetaiotaomicron in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NA7
Type: protein
Length: 647 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative dipeptidyl-peptidase III
EC: 3.4.14.4
UniProt: Q8A6N1
Ligands: ZN, CL, SO4
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative dipeptidyl-peptidase III (EC 3.4.14.4)	protein	647	50% helix, 14% strand	Q8A6N1

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1190	0.74	0.77	72	CL
2	89	0.60	0.88	24	empty
3	158	0.57	0.81	30	CL
4	220	0.52	0.77	28	empty
5	72	0.42	0.80	19	CL

Compared structures

5NA7 · Structure of DPP III from Bacteroides thetaiotaomicron · 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 Q8A6N1
Elsewhere: RCSB PDB 5NA7 · PDBe 5NA7 · UniProt Q8A6N1

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