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Structure of 6-aminohexanoate cyclic dimer hydrolase

Analyse Structure of 6-aminohexanoate cyclic dimer hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3A2P
Type: protein
Length: 483 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 6-aminohexanoate-cyclic-dimer hydrolase
EC: 3.5.2.12
UniProt: P13398
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12)	protein	483	42% helix, 14% strand	P13398

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.79	0.97	29	empty
2	72	0.63	0.92	24	empty
3	61	0.46	0.84	23	empty
4	54	0.27	0.74	16	empty

Compared structures

3A2P · Structure of 6-aminohexanoate cyclic dimer hydrolase · the same entry in another collection · chain A against A, TM-score 1.00
P13398 · AlphaFold monomer V2.0 prediction for 6-aminohexanoate-cyclic-dimer hydrolase (P13398) · a predicted model of the same protein · 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 P13398
Elsewhere: RCSB PDB 3A2P · PDBe 3A2P · UniProt P13398

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