MolNFT v1 · #129106 · protein

Structure of the DMPAR3 PDZ1 domain in complex with the DMPAR6 pbm

5OAK · Bazooka, isoform C,LD29223P: “Structure of the DMPAR3 PDZ1 domain in complex with the DMPAR6 pbm”. X-ray diffraction, 2 pockets (best druggability 0.42). MolNFT v1 #129106 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5OAK
Type: protein
Length: 202 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bazooka, isoform C,LD29223P
UniProt: X2JFU8, O97111
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Bazooka, isoform C,LD29223P	protein	90	17% helix, 34% strand	X2JFU8, O97111
B, D	Bazooka, isoform C,LD29223P	protein	11	0% helix, 45% strand	X2JFU8, O97111

Ligands and binding sites

GOL · Glycerol · additive · chains A, C

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.42	0.80	17	empty
2	81	0.39	0.77	27	empty

Interfaces

4 interfaces between chains.

C–D · 471 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 466 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 317 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 201 Å² buried · 1 hydrogen bond · protein-protein

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 X2JFU8
Every structure of UniProt O97111
Elsewhere: RCSB PDB 5OAK · PDBe 5OAK · UniProt X2JFU8 · UniProt O97111

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