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Solution structure of the complex of mutant VEK50[RH2/AA] and plasminogen kringle 2

Analyse Solution structure of the complex of mutant VEK50[RH2/AA] and plasminogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OQK
Type: protein
Length: 139 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasminogen kringle 2; Plasminogen-binding group a streptococcal M-like protein pam
UniProt: P49054
Pockets: 1 · best druggability 0.50

Structure

solution nmr · 2 distinct chains · 32% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plasminogen kringle 2	protein	87	7% helix, 17% strand	—
B	Plasminogen-binding group a streptococcal M-like protein pam	protein	52	73% helix, 0% strand	P49054

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.50	0.75	28	empty

Interfaces

1 interface between chains.

A–B · 851 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

6OQK · Solution structure of the complex of mutant VEK50[RH2/AA] and plasminogen kringle 2 · the same entry in another collection · chain A against A, TM-score 1.00
P49054 · AlphaFold monomer V2.0 prediction for plasminogen-binding group a streptococcal M-like… · a predicted model of the same protein · chain B against A, TM-score 0.51

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 P49054
Elsewhere: RCSB PDB 6OQK · PDBe 6OQK · UniProt P49054

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