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Beta domain of streptokinase

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

PDB: 1C4P
Type: protein
Length: 538 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (streptokinase)
UniProt: Q53284
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (streptokinase)	protein	137	11% helix, 41% strand	Q53284
C, D	Protein (streptokinase)	protein	132	11% helix, 46% strand	Q53284

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	958	0.80	0.82	105	empty
2	740	0.79	0.83	89	empty
3	250	0.52	0.75	31	empty
4	228	0.51	0.76	33	empty
5	75	0.51	0.85	21	empty

Interfaces

5 interfaces between chains.

B–D · 1427 Å² buried · 22 hydrogen bonds · protein-protein
A–C · 1370 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 544 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 479 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 445 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1C4P · Beta domain of streptokinase · 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 Q53284
Elsewhere: RCSB PDB 1C4P · PDBe 1C4P · UniProt Q53284

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