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Crystal structure of an amidohydrolase GI:44264246 from an evironmental sample of sargasso sea

Analyse Crystal structure of an amidohydrolase GI:44264246 from an evironmental sample… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HPA
Type: protein
Length: 856 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase
Ligands: ZN
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Amidohydrolase	protein	428	40% helix, 22% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

7 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	68	0.72	0.97	27	empty
2	245	0.65	0.83	32	empty
3	491	0.65	0.77	51	empty
4	213	0.65	0.83	30	empty
5	100	0.33	0.72	21	empty

Interfaces

1 interface between chains.

A–B · 2208 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

3HPA · Crystal structure of an amidohydrolase gi:44264246 from an evironmental sample of… · 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
Elsewhere: RCSB PDB 3HPA · PDBe 3HPA

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