4YWA
Structural Insight into Divalent Galactoside Binding to Pseudomonas aeruginosa lectin LecA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
A | 0009986 | cellular_component | cell surface |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0042597 | cellular_component | periplasmic space |
B | 0005737 | cellular_component | cytoplasm |
B | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
B | 0009986 | cellular_component | cell surface |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0042597 | cellular_component | periplasmic space |
C | 0005737 | cellular_component | cytoplasm |
C | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
C | 0009986 | cellular_component | cell surface |
C | 0030246 | molecular_function | carbohydrate binding |
C | 0042597 | cellular_component | periplasmic space |
D | 0005737 | cellular_component | cytoplasm |
D | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
D | 0009986 | cellular_component | cell surface |
D | 0030246 | molecular_function | carbohydrate binding |
D | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 201 |
Chain | Residue |
A | TYR36 |
A | ASP100 |
A | THR104 |
A | ASN107 |
A | ASN108 |
A | 4J9202 |
site_id | AC2 |
Number of Residues | 32 |
Details | binding site for residue 4J9 A 202 |
Chain | Residue |
A | GLN53 |
A | ASP100 |
A | THR104 |
A | ASN107 |
A | CA201 |
A | HOH302 |
A | HOH304 |
A | HOH308 |
A | HOH310 |
A | HOH318 |
A | HOH319 |
A | HOH321 |
A | HOH323 |
A | HOH330 |
A | HOH343 |
A | HOH355 |
A | HOH364 |
A | HOH374 |
A | HOH409 |
B | TYR36 |
B | HIS50 |
B | GLN53 |
B | ASP100 |
B | THR104 |
B | ASN107 |
B | CA900 |
B | HOH1012 |
B | HOH1039 |
B | HOH1048 |
A | TYR36 |
A | GLN40 |
A | HIS50 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA B 900 |
Chain | Residue |
A | 4J9202 |
B | TYR36 |
B | ASP100 |
B | THR104 |
B | ASN107 |
B | ASN108 |
site_id | AC4 |
Number of Residues | 31 |
Details | binding site for residue 4J9 C 201 |
Chain | Residue |
C | TYR36 |
C | GLN40 |
C | HIS50 |
C | GLN53 |
C | ASP100 |
C | THR104 |
C | ASN107 |
C | CA202 |
C | HOH304 |
C | HOH312 |
C | HOH313 |
C | HOH315 |
C | HOH320 |
C | HOH321 |
C | HOH331 |
C | HOH350 |
C | HOH353 |
C | HOH362 |
C | HOH368 |
C | HOH418 |
D | TYR36 |
D | GLU49 |
D | HIS50 |
D | GLN53 |
D | ASP100 |
D | THR104 |
D | ASN107 |
D | CA900 |
D | HOH1012 |
D | HOH1031 |
D | HOH1045 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA C 202 |
Chain | Residue |
C | TYR36 |
C | ASP100 |
C | THR104 |
C | ASN107 |
C | ASN108 |
C | 4J9201 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA D 900 |
Chain | Residue |
C | 4J9201 |
D | TYR36 |
D | ASP100 |
D | THR104 |
D | ASN107 |
D | ASN108 |