Functional Information from GO Data
Chain | GOid | namespace | contents |
M | 0005618 | cellular_component | cell wall |
N | 0005618 | cellular_component | cell wall |
O | 0005618 | cellular_component | cell wall |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue GOL L 301 |
Chain | Residue |
H | PHE174 |
L | THR178 |
H | PRO175 |
H | SER186 |
H | LEU187 |
H | SER188 |
L | GLN160 |
L | SER162 |
L | SER176 |
L | SER177 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue GOL L 302 |
Chain | Residue |
H | VAL171 |
H | HIS172 |
H | THR173 |
L | THR164 |
L | GLU165 |
L | ASP167 |
L | HOH425 |
L | HOH434 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL L 303 |
Chain | Residue |
C | SER29 |
C | SER30 |
L | TYR32 |
L | THR93 |
L | SER94 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue GOL L 304 |
Chain | Residue |
L | ASP170 |
L | SER171 |
L | HOH407 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL L 305 |
Chain | Residue |
L | GLN37 |
L | GLN38 |
L | LYS39 |
L | GLN42 |
L | ALA43 |
L | ARG45 |
L | HOH401 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL H 301 |
Chain | Residue |
H | ARG38 |
H | GLN39 |
H | ALA40 |
H | GLN43 |
H | GLY44 |
H | GLU46 |
H | LYS62 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL H 302 |
Chain | Residue |
H | GLU150 |
H | PRO151 |
H | VAL152 |
H | PHE174 |
H | PRO175 |
H | ALA176 |
H | LEU187 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | SER162 |
A | SER176 |
A | SER177 |
A | THR178 |
B | PHE174 |
B | PRO175 |
B | SER186 |
B | LEU187 |
B | SER188 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
A | THR164 |
A | GLU165 |
A | ASP167 |
B | HIS172 |
B | THR173 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL C 301 |
Chain | Residue |
C | GLN160 |
C | SER162 |
C | SER176 |
C | THR178 |
D | PHE174 |
D | PRO175 |
D | SER186 |
D | LEU187 |
D | SER188 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue GOL C 302 |
Chain | Residue |
C | TYR87 |
C | GLN100 |
D | GLY42 |
D | GLN43 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL D 301 |
Chain | Residue |
D | LYS117 |
D | GLY118 |
N | THR21 |
N | THR22 |
N | TYR38 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL O 101 |
Chain | Residue |
B | LYS117 |
B | GLY118 |
O | THR21 |
O | THR22 |
O | TYR38 |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
Chain | Residue | Details |
L | TYR192-HIS198 | |
H | TYR206-HIS212 | |