MolNFT v1 · #113798 · protein

Darpin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein crystallography

5AQ9 · OFF7_DB08V4: “Darpin-based crystallization chaperones exploit molecular geometry as a screening dimension in protein…”. X-ray diffraction, 15 pockets (best druggability 0.79). MolNFT v1 #113798 on GenesisL1: 3D structure, binding…

PDB: 5AQ9
Type: protein
Length: 1,580 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: OFF7_DB08V4; Maltose-binding periplasmic protein
UniProt: P0AEX9
Pockets: 15 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	OFF7_DB08V4	protein	419	47% helix, 11% strand	—
B, D	Maltose-binding periplasmic protein	protein	371	44% helix, 21% strand	P0AEX9

Pockets

15 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	1039	0.79	0.80	81	empty
2	935	0.71	0.76	80	empty
3	339	0.66	0.80	29	empty
4	381	0.66	0.79	35	empty
5	337	0.58	0.76	45	empty

Interfaces

4 interfaces between chains.

A–B · 757 Å² buried · 7 hydrogen bonds · protein-protein
C–D · 741 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 514 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 40 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 P0AEX9
Elsewhere: RCSB PDB 5AQ9 · PDBe 5AQ9 · UniProt P0AEX9

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