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 |
C | 0005886 | cellular_component | plasma membrane |
C | 0008658 | molecular_function | penicillin binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0042597 | cellular_component | periplasmic space |
C | 0046677 | biological_process | response to antibiotic |
C | 0071555 | biological_process | cell wall organization |
D | 0005886 | cellular_component | plasma membrane |
D | 0008658 | molecular_function | penicillin binding |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0042597 | cellular_component | periplasmic space |
D | 0046677 | biological_process | response to antibiotic |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AUC E 1 |
Chain | Residue |
A | ALA66 |
A | SER67 |
A | PHE69 |
A | LYS70 |
A | ASN73 |
A | PHE120 |
A | TRP154 |
A | HOH401 |
A | HOH558 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AUC E 2 |
Chain | Residue |
B | ALA66 |
B | SER67 |
B | PHE69 |
B | LYS70 |
B | ASN73 |
B | PHE120 |
B | TRP154 |
B | HOH569 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE AUC E 3 |
Chain | Residue |
C | LYS70 |
C | ALA116 |
C | VAL117 |
C | TRP154 |
C | HOH434 |
C | AUC302 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AUC E 4 |
Chain | Residue |
B | LYS95 |
B | HOH515 |
C | ALA66 |
C | SER67 |
C | LYS70 |
C | ASN73 |
C | PHE120 |
C | TRP154 |
C | AUC301 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AUC E 5 |
Chain | Residue |
C | GLN133 |
C | HOH410 |
C | EDO308 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AUC E 6 |
Chain | Residue |
D | ALA66 |
D | SER67 |
D | LYS70 |
D | ASN73 |
D | PHE120 |
D | TRP154 |
D | AUC302 |
D | HOH542 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE AUC E 7 |
Chain | Residue |
D | LYS70 |
D | ALA116 |
D | VAL117 |
D | TRP154 |
D | HOH454 |
D | AUC301 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AUC E 8 |
Chain | Residue |
D | GLN133 |
D | HOH452 |
D | HOH539 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 E 9 |
Chain | Residue |
A | SER115 |
A | THR206 |
A | GLY207 |
A | PHE208 |
A | ARG250 |
A | HOH500 |
A | HOH469 |
A | HOH411 |
A | HOH498 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 10 |
Chain | Residue |
A | ARG131 |
A | LYS134 |
A | TYR135 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 E 11 |
Chain | Residue |
A | ARG160 |
A | HOH542 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 12 |
Chain | Residue |
A | ILE22 |
C | SER33 |
C | ALA36 |
C | VAL37 |
C | ASN38 |
C | EDO307 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 E 13 |
Chain | Residue |
B | SER115 |
B | LYS205 |
B | THR206 |
B | GLY207 |
B | PHE208 |
B | ARG250 |
B | HOH464 |
B | HOH577 |
B | HOH450 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 14 |
Chain | Residue |
B | MET99 |
B | LYS100 |
B | GLN101 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 15 |
Chain | Residue |
B | GLU35 |
B | SER245 |
B | LYS246 |
B | HOH432 |
B | HOH401 |
B | HOH433 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 16 |
Chain | Residue |
B | PRO198 |
B | GLU199 |
B | LEU201 |
B | GLU227 |
B | GLU229 |
D | THR107 |
D | ARG109 |
B | HOH560 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 E 17 |
Chain | Residue |
C | SER67 |
C | THR206 |
C | GLY207 |
C | PHE208 |
C | ARG250 |
C | HOH505 |
B | LYS95 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 18 |
Chain | Residue |
A | HOH425 |
A | HOH436 |
C | SER181 |
C | LYS182 |
C | HOH517 |
C | HOH514 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 19 |
Chain | Residue |
A | LYS95 |
D | SER67 |
D | THR206 |
D | GLY207 |
D | PHE208 |
D | ARG250 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 20 |
Chain | Residue |
B | GLU183 |
B | HOH516 |
B | HOH466 |
D | SER181 |
D | LYS182 |
D | HOH464 |
D | HOH561 |
D | HOH506 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 21 |
Chain | Residue |
D | THR213 |
D | SER215 |
D | ASN216 |
D | HOH523 |
D | HOH501 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 22 |
Chain | Residue |
A | GLY128 |
A | GLU129 |
A | VAL130 |
A | HOH518 |
A | HOH402 |
A | HOH526 |
site_id | CC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 E 23 |
Chain | Residue |
A | THR107 |
A | ARG109 |
C | PRO198 |
C | GLU199 |
C | LEU201 |
C | GLU227 |
C | GLU229 |
C | HOH452 |
A | HOH553 |
A | HOH508 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO E 24 |
Chain | Residue |
C | GLU195 |
C | TYR200 |
C | HOH612 |
site_id | CC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO E 25 |
Chain | Residue |
C | ASN29 |
C | PHE32 |
C | VAL37 |
C | ASN38 |
C | GLY39 |
C | ASN54 |
C | HOH408 |
A | SO4305 |
C | HOH441 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 26 |
Chain | Residue |
B | ASN29 |
B | VAL37 |
B | ASN38 |
B | GLY39 |
B | ASN54 |
B | HOH565 |
site_id | CC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO E 27 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 28 |
Chain | Residue |
B | THR107 |
B | ARG109 |
D | PRO198 |
D | GLU199 |
D | GLU229 |
D | HOH433 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO E 29 |
Chain | Residue |
B | THR80 |
B | ARG131 |
B | LYS134 |
B | TYR135 |
B | HOH493 |
site_id | DC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 30 |
Chain | Residue |
A | GLU199 |
A | GLU227 |
A | GLU229 |
C | THR107 |
C | HOH438 |
A | HOH447 |
A | HOH520 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 31 |
Chain | Residue |
C | ILE146 |
C | SER147 |
C | GLY148 |
C | GLY149 |
C | ILE150 |
C | AUC303 |
site_id | DC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 32 |
Chain | Residue |
A | ALA36 |
A | PRO217 |
A | ASP240 |
A | ASP242 |
A | HOH409 |
A | HOH413 |
A | HOH434 |
site_id | DC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 33 |
Chain | Residue |
B | GLU195 |
B | TYR200 |
B | VAL202 |
B | MET258 |
B | GLU259 |
B | ILE263 |
B | HOH416 |
site_id | DC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO E 34 |
Chain | Residue |
B | PRO217 |
B | ASP240 |
B | HOH453 |
B | HOH403 |
B | HOH402 |
site_id | DC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO E 35 |
Chain | Residue |
B | ASN143 |
B | ASN145 |
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 | |
D | PRO65-ILE75 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
D | SER67 | |
B | SER67 | |
C | SER67 | |
Chain | Residue | Details |
D | SER115 | |
C | THR206 | |
C | PHE208 | |
C | ARG250 | |
D | THR206 | |
D | PHE208 | |
D | ARG250 | |
B | SER115 | |
B | THR206 | |
B | PHE208 | |
B | ARG250 | |
C | SER115 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11188693, ECO:0000269|PubMed:11724923, ECO:0000269|PubMed:19860471, ECO:0007744|PDB:1E4D, ECO:0007744|PDB:1K4E, ECO:0007744|PDB:1K4F, ECO:0007744|PDB:1K54, ECO:0007744|PDB:1K55, ECO:0007744|PDB:1K56, ECO:0007744|PDB:1K57, ECO:0007744|PDB:1K6S, ECO:0007744|PDB:2RL3 |
Chain | Residue | Details |
D | LYS70 | |
B | LYS70 | |
C | LYS70 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1m6k |
Chain | Residue | Details |
D | SER67 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1m6k |
Chain | Residue | Details |
A | SER67 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1m6k |
Chain | Residue | Details |
B | SER67 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1m6k |
Chain | Residue | Details |
C | SER67 | |