Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
B | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
C | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
D | 0008270 | molecular_function | zinc ion 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 302 |
Chain | Residue |
A | ASN150 |
A | LYS167 |
A | ARG169 |
D | LYS148 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 901 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS196 |
A | MCO811 |
A | ZN902 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 902 |
Chain | Residue |
A | ASP120 |
A | CYS221 |
A | HIS263 |
A | MCO811 |
A | ZN901 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 901 |
Chain | Residue |
B | HIS116 |
B | HIS118 |
B | HIS196 |
B | MCO812 |
B | ZN902 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 902 |
Chain | Residue |
B | ASP120 |
B | CYS221 |
B | HIS263 |
B | MCO812 |
B | ZN901 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 901 |
Chain | Residue |
C | HIS116 |
C | HIS118 |
C | HIS196 |
C | MCO813 |
C | ZN902 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 902 |
Chain | Residue |
C | ASP120 |
C | CYS221 |
C | HIS263 |
C | MCO813 |
C | ZN901 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 901 |
Chain | Residue |
D | HIS116 |
D | HIS118 |
D | HIS196 |
D | MCO814 |
D | ZN902 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 902 |
Chain | Residue |
D | ASP120 |
D | CYS221 |
D | HIS263 |
D | MCO814 |
D | ZN901 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 900 |
Chain | Residue |
A | HIS285 |
A | ASP288 |
A | HOH1084 |
A | HOH1085 |
A | HOH1086 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 900 |
Chain | Residue |
A | HOH1087 |
B | HIS285 |
B | ASP288 |
B | HOH1070 |
B | HOH1071 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 900 |
Chain | Residue |
C | HIS285 |
C | ASP288 |
C | HOH1074 |
C | HOH1075 |
D | HOH1089 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 900 |
Chain | Residue |
D | HIS285 |
D | ASP288 |
D | HOH1090 |
D | HOH1091 |
D | HOH1092 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MCO A 811 |
Chain | Residue |
A | TYR100 |
A | HIS118 |
A | ASP119 |
A | ASP120 |
A | LYS167 |
A | HIS196 |
A | TYR233 |
A | ZN901 |
A | ZN902 |
A | HOH985 |
A | HOH996 |
A | HOH1073 |
site_id | BC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MCO B 812 |
Chain | Residue |
B | HIS118 |
B | ASP119 |
B | ASP120 |
B | LYS167 |
B | HIS196 |
B | TYR233 |
B | ZN901 |
B | ZN902 |
B | HOH1012 |
B | HOH1049 |
B | HOH1069 |
D | TYR100 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MCO C 813 |
Chain | Residue |
B | TYR100 |
C | HIS118 |
C | ASP119 |
C | ASP120 |
C | LYS167 |
C | HIS196 |
C | TYR233 |
C | ZN901 |
C | ZN902 |
C | HOH1010 |
C | HOH1048 |
site_id | BC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MCO D 814 |
Chain | Residue |
C | TYR100 |
D | HIS118 |
D | ASP119 |
D | ASP120 |
D | LYS167 |
D | HIS196 |
D | TYR233 |
D | ZN901 |
D | ZN902 |
D | HOH977 |
D | HOH1034 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 801 |
Chain | Residue |
A | GLY235 |
A | GLU236 |
A | ALA237 |
A | TYR238 |
A | HOH950 |
A | HOH1023 |
B | GLN171 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 802 |
Chain | Residue |
B | GLY235 |
B | GLU236 |
B | ALA237 |
B | HOH933 |
B | HOH1025 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 803 |
Chain | Residue |
C | GLN171 |
C | GLY235 |
C | GLU236 |
C | ALA237 |
C | HOH970 |
C | HOH1006 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 804 |
Chain | Residue |
A | GLN171 |
D | GLY235 |
D | GLU236 |
D | ALA237 |
D | TYR238 |
D | HOH1030 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IaTHsHDDraGGleyfgki.G |
Chain | Residue | Details |
A | ILE113-GLY133 | |
site_id | PS00744 |
Number of Residues | 13 |
Details | BETA_LACTAMASE_B_2 Beta-lactamases class B signature 2. PkekVLvGgCIIK |
Chain | Residue | Details |
A | PRO209-LYS224 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
B | ASP120 | |
B | HIS196 | |
B | CYS221 | |
B | LYS224 | |
B | HIS263 | |
C | HIS116 | |
C | HIS118 | |
C | ASP120 | |
C | HIS196 | |
C | CYS221 | |
A | HIS118 | |
C | LYS224 | |
C | HIS263 | |
D | HIS116 | |
D | HIS118 | |
D | ASP120 | |
D | HIS196 | |
D | CYS221 | |
D | LYS224 | |
D | HIS263 | |
A | ASP120 | |
A | HIS196 | |
A | CYS221 | |
A | LYS224 | |
A | HIS263 | |
B | HIS116 | |
B | HIS118 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
A | ASP120 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
B | ASP120 | |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
C | ASP120 | |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qh5 |
Chain | Residue | Details |
D | ASP120 | |