Execution time: 10.0 seconds
Match RMSD = 0.53
VTR = 0.01
Average AVD = 0.41 Å
Chains(7KLG.pdb ): B versus I
Chains(7KLG_africa_mut.pdb ) B versus I
Cutoff: 2 Å
Detection of structural contacts in α-helices OFF
Contacts found | Number of residues | Hydrophobic | Attractive | Hydrogen Bonds | Disulphide Bonds | Repulsive | Aromatic Stacking | Total |
---|---|---|---|---|---|---|---|---|
A7KLG | 1269 | 29 | 0 | 2 | 0 | 0 | 1 | 32 |
B7KLG_africa_mut | 1269 | 36 | 0 | 2 | 0 | 0 | 1 | 39 |
(Conservatives hydrophobic matches are hidden by default)
Chains | Residues | Contact types | |||||||
---|---|---|---|---|---|---|---|---|---|
A | B | A1 | A2 | B1 | B2 | A [1-2] | B [1-2] | AVD | Contact |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.2 | View |
I-B | I-B | F113 | L455 | F113 | L455 | Hydrophobic | Hydrophobic | 0.49 | View |
I-B | I-B | Y109 | Y489 | Y109 | Y489 | Hydrophobic | Hydrophobic | 0.63 | View |
I-B | I-B | F113 | Q493 | F113 | Q493 | Hydrophobic | Hydrophobic | 0.22 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.31 | View |
I-B | I-B | Y109 | E484 | Y109 | K484 | Hydrogen Bonds | Hydrogen Bonds | 1.8 | View |
I-B | I-B | Y109 | Y489 | Y109 | Y489 | Hydrophobic | Hydrophobic | 0.84 | View |
I-B | I-B | Y109 | Y489 | Y109 | Y489 | Hydrophobic | Hydrophobic | 0.46 | View |
I-B | I-B | Y109 | Y489 | Y109 | Y489 | Hydrophobic | Hydrophobic | 0.64 | View |
I-B | I-B | F113 | Q493 | F113 | Q493 | Hydrophobic | Hydrophobic | 0.29 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.3 | View |
I-B | I-B | Y109 | Y489 | Y109 | Y489 | Hydrophobic | Hydrophobic | 0.67 | View |
I-B | I-B | F113 | Q493 | F113 | Q493 | Hydrophobic | Hydrophobic | 0.26 | View |
I-B | I-B | A64 | F486 | A64 | F486 | Hydrophobic | Hydrophobic | 0.34 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Aromatic Stacking | Aromatic Stacking | 0.11 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.24 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.15 | View |
I-B | I-B | Y109 | F490 | Y109 | F490 | Hydrogen Bonds | Hydrogen Bonds | 1.14 | View |
I-B | I-B | Y110 | E484 | Y110 | K484 | Hydrophobic | Hydrophobic | 0.47 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.21 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.2 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.26 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.26 | View |
I-B | I-B | Y110 | Y489 | Y110 | Y489 | Hydrophobic | Hydrophobic | 0.36 | View |
I-B | I-B | F113 | L455 | F113 | L455 | Hydrophobic | Hydrophobic | 0.46 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.15 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.21 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.24 | View |
I-B | I-B | A66 | F486 | A66 | F486 | Hydrophobic | Hydrophobic | 0.19 | View |
I-B | I-B | Y110 | F486 | Y110 | F486 | Hydrophobic | Hydrophobic | 0.16 | View |
I-B | I-B | F113 | L455 | F113 | L455 | Hydrophobic | Hydrophobic | 0.48 | View |
I-B | I-B | Y110 | Y489 | Y110 | Y489 | Hydrophobic | Hydrophobic | 0.36 | View |
Protein | Chains | Residue1 | Residue2 | Contact types | Distance | Contact |
---|---|---|---|---|---|---|
7KLG_africa_mut | I-B | A64 | F486 | Hydrophobic | 4.40 | View |
7KLG_africa_mut | I-B | Y109 | K484 | Hydrophobic | 4.02 | View |
7KLG_africa_mut | I-B | Y110 | K484 | Hydrophobic | 3.78 | View |
7KLG_africa_mut | I-B | Y110 | K484 | Hydrophobic | 3.67 | View |
7KLG_africa_mut | I-B | Y110 | K484 | Hydrophobic | 3.50 | View |
7KLG_africa_mut | I-B | Y110 | K484 | Hydrophobic | 3.69 | View |
7KLG_africa_mut | I-B | Y110 | F486 | Hydrophobic | 4.23 | View |
Residue Match Frequency | View |
---|---|
GLU | |
ALA | |
TYR | |
THR | |
LEU | |
SER | |
PHE | |
GLY | |
MET | |
PRO | |
LYS | |
VAL | |
HIS | |
ILE | |
CYS | |
ARG | |
GLN | |
ASP | |
ASN | |
TRP |