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Amidohydrolase, ahs

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

PDB: 6SJ0
Type: protein
Length: 986 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase
UniProt: A0A022MQ12
Ligands: BCT, ZN, SO4
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidohydrolase	protein	493	41% helix, 19% strand	A0A022MQ12
B	Amidohydrolase	protein	493	40% helix, 19% strand	A0A022MQ12

Ligands and binding sites

BCT · Bicarbonate ion · ligand · chains A
ZN · Zinc ion · metal · 22 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · 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, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.79	0.87	73	empty
2	75	0.75	0.98	27	empty
3	375	0.73	0.84	46	PEG
4	218	0.67	0.84	23	ZN
5	273	0.66	0.82	25	empty

Interfaces

1 interface between chains.

A–B · 3669 Å² buried · 59 hydrogen bonds · protein-protein

Compared structures

6SJ0 · Amidohydrolase, AHS · 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 6SJ0 · PDBe 6SJ0 · UniProt A0A022MQ12

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