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Amidohydrolase, ahs with 3-haa

Analyse Amidohydrolase, ahs with 3-haa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SJ2
Type: protein
Length: 998 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase
UniProt: A0A022MQ12
Ligands: 3HA, ZN, MG
Pockets: 9 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidohydrolase	protein	495	41% helix, 19% strand	A0A022MQ12
B	Amidohydrolase	protein	503	41% helix, 19% strand	A0A022MQ12

Ligands and binding sites

3HA · 3-hydroxyanthranilic acid · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
MG · Magnesium ion · metal · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

9 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	450	0.80	0.87	72	3HA
2	483	0.79	0.86	74	3HA
3	715	0.74	0.80	81	empty
4	243	0.65	0.83	27	empty
5	100	0.45	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 3644 Å² buried · 59 hydrogen bonds · protein-protein

Compared structures

6SJ2 · Amidohydrolase, AHS with 3-HAA · 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 A0A022MQ12
Elsewhere: RCSB PDB 6SJ2 · PDBe 6SJ2 · UniProt A0A022MQ12

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