4KI3
1.70 Angstrom resolution crystal structure of outer-membrane lipoprotein carrier protein (lolA) from Yersinia pestis CO92
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042953 | biological_process | lipoprotein transport |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042953 | biological_process | lipoprotein transport |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042953 | biological_process | lipoprotein transport |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042953 | biological_process | lipoprotein transport |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0042953 | biological_process | lipoprotein transport |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0042953 | biological_process | lipoprotein transport |
| G | 0042597 | cellular_component | periplasmic space |
| G | 0042953 | biological_process | lipoprotein transport |
| H | 0042597 | cellular_component | periplasmic space |
| H | 0042953 | biological_process | lipoprotein transport |
| I | 0042597 | cellular_component | periplasmic space |
| I | 0042953 | biological_process | lipoprotein transport |
| J | 0042597 | cellular_component | periplasmic space |
| J | 0042953 | biological_process | lipoprotein transport |
| K | 0042597 | cellular_component | periplasmic space |
| K | 0042953 | biological_process | lipoprotein transport |
| L | 0042597 | cellular_component | periplasmic space |
| L | 0042953 | biological_process | lipoprotein transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 301 |
| Chain | Residue |
| A | SER155 |
| A | THR157 |
| A | HOH514 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 302 |
| Chain | Residue |
| A | GLN28 |
| A | ASN29 |
| A | SER32 |
| A | HOH486 |
| B | TRP101 |
| B | LYS103 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | LEU87 |
| A | PHE89 |
| A | THR106 |
| A | ASN108 |
| A | MET112 |
| A | HOH452 |
| A | HOH515 |
| B | SER48 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 301 |
| Chain | Residue |
| B | ASP26 |
| B | ASN29 |
| B | LYS33 |
| D | ARG202 |
| D | HOH504 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 301 |
| Chain | Residue |
| A | THR191 |
| A | HOH535 |
| D | SER155 |
| D | THR157 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG D 302 |
| Chain | Residue |
| A | ARG202 |
| A | HOH538 |
| D | ASP26 |
| D | ASN29 |
| D | ARG30 |
| D | LYS33 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT F 301 |
| Chain | Residue |
| F | ASN66 |
| F | ARG116 |
| F | ASN118 |
| F | HOH462 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT G 301 |
| Chain | Residue |
| G | LEU87 |
| G | THR106 |
| G | ASN108 |
| G | MET112 |
| H | HOH469 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT H 301 |
| Chain | Residue |
| H | ASN108 |
| H | HOH464 |
| I | SER48 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL H 302 |
| Chain | Residue |
| H | SER36 |
| I | SER186 |
| I | THR189 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT I 301 |
| Chain | Residue |
| I | LYS159 |
| I | THR174 |
| I | LEU175 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG J 301 |
| Chain | Residue |
| J | THR46 |
| J | SER47 |
| J | SER48 |
| J | GLY50 |
| J | ARG170 |
| L | LEU87 |
| L | PHE89 |
