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The crystal structure of lobster apocrustacyanin A1 using softer X- rays.

Analyse The crystal structure of lobster apocrustacyanin A1 using softer X- rays. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H91
Type: protein
Length: 360 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Crustacyanin A1 subunit
Pockets: 6 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Crustacyanin A1 subunit	protein	180	19% helix, 42% strand	—

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains A, B

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

Pockets

6 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	192	0.82	0.96	26	MPD
2	474	0.81	0.88	61	MPD
3	138	0.56	0.83	20	empty
4	150	0.55	0.80	21	empty
5	56	0.31	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1142 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 1 covalent (disulfide, additive adduct).

Compared structures

1H91 · The crystal structure of lobster apocrustacyanin A1 using softer X-rays. · 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 1H91 · PDBe 1H91

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