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On the routine use of soft X-rays in macromolecular crystallography, part III- the optimal data collection wavelength

Analyse On the routine use of soft X-rays in macromolecular crystallography, part III… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A7G
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermolysin
EC: 2.2.1.2
UniProt: P00800
Ligands: CA, ZN
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E	Thermolysin (EC 2.2.1.2)	protein	316	41% helix, 18% strand	P00800

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains E
ZN · Zinc ion · metal · chains E
DMS · Dimethyl sulfoxide · additive · 2 copies · chains E
ACY · Acetic acid · additive · chains E

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.44	0.78	23	ACY
2	52	0.35	0.79	13	empty

Compared structures

2A7G · On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The… · the same entry in another collection · chain E against E, 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 P00800
Elsewhere: RCSB PDB 2A7G · PDBe 2A7G · UniProt P00800

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