2RL3
Crystal structure of the OXA-10 W154H mutant at pH 7
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0071555 | biological_process | cell wall organization |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | GOL8 |
| A | HOH364 |
| A | SER67 |
| A | SER115 |
| A | LYS205 |
| A | THR206 |
| A | GLY207 |
| A | PHE208 |
| A | ARG250 |
| A | HOH300 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 4 |
| Chain | Residue |
| A | LYS134 |
| A | LYS138 |
| A | LYS152 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 11 |
| Chain | Residue |
| A | ARG250 |
| A | HOH346 |
| A | HOH454 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2 |
| Chain | Residue |
| B | SER115 |
| B | THR206 |
| B | GLY207 |
| B | PHE208 |
| B | ARG250 |
| B | HOH372 |
| B | HOH396 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3 |
| Chain | Residue |
| B | THR80 |
| B | ARG131 |
| B | LYS134 |
| B | TYR135 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 12 |
| Chain | Residue |
| A | ARG160 |
| A | HOH446 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | GOL9 |
| A | MET99 |
| A | LYS100 |
| A | SER147 |
| A | GLY148 |
| A | GLY149 |
| A | HOH277 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 8 |
| Chain | Residue |
| A | SO41 |
| A | SER67 |
| A | TRP102 |
| A | SER115 |
| A | VAL117 |
| A | GLU129 |
| A | PHE208 |
| A | HOH300 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 9 |
| Chain | Residue |
| A | GOL7 |
| A | ALA98 |
| A | MET99 |
| A | GLU129 |
| A | ILE146 |
| A | GLY149 |
| A | ILE150 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 13 |
| Chain | Residue |
| A | LYS138 |
| A | PHE139 |
| A | SER140 |
| A | GLU168 |
| A | SER172 |
| A | HOH283 |
| A | HOH434 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 5 |
| Chain | Residue |
| A | PRO198 |
| A | GLU199 |
| A | GLU227 |
| A | GLU229 |
| A | HOH343 |
| B | THR107 |
| B | ARG109 |
| B | GLY110 |
| B | HOH330 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 6 |
| Chain | Residue |
| B | LEU43 |
| B | SER50 |
| B | TYR233 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 10 |
| Chain | Residue |
| B | LEU247 |
| B | PRO248 |
| B | ARG250 |
| B | LYS251 |
| B | HOH355 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI |
| Chain | Residue | Details |
| A | PRO65-ILE75 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"11188693","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11724923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19860471","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K4F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K55","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K56","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RL3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1m6k |
| Chain | Residue | Details |
| A | SER67 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1m6k |
| Chain | Residue | Details |
| B | SER67 |
