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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS196 |
A | MP21410 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | ASP120 |
A | HIS121 |
A | HIS263 |
A | MP21410 |
A | HOH1641 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | HIS116 |
B | HIS118 |
B | HIS196 |
B | MP22410 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | ASP120 |
B | HIS121 |
B | HIS263 |
B | MP22410 |
B | HOH2580 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1 |
Chain | Residue |
B | ARG172 |
B | VAL179 |
B | ILE180 |
B | THR181 |
B | HOH2479 |
B | HOH2573 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 2 |
Chain | Residue |
A | ARG172 |
A | VAL179 |
A | ILE180 |
A | THR181 |
A | HOH1587 |
A | HOH1687 |
A | HOH1716 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 3 |
Chain | Residue |
A | ARG252 |
A | LYS297 |
A | HOH1518 |
A | HOH1528 |
B | ARG209 |
B | ALA275 |
B | ARG276 |
B | ALA289 |
B | GLY290 |
B | ALA291 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | ARG209 |
A | ALA275 |
A | ARG276 |
A | ALA289 |
A | GLY290 |
A | ALA291 |
A | HOH1543 |
A | HOH1563 |
B | ARG252 |
B | LYS297 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | ARG252 |
A | HOH1721 |
B | ARG209 |
B | ASN210 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 6 |
Chain | Residue |
A | ARG102 |
A | ASN210 |
A | HOH1494 |
A | HOH1549 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 7 |
Chain | Residue |
B | ARG102 |
B | GLY211 |
B | HOH2602 |
site_id | BC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MP2 A 1410 |
Chain | Residue |
A | TYR33 |
A | TRP39 |
A | ASP120 |
A | PHE156 |
A | GLY161 |
A | ILE162 |
A | HIS196 |
A | SER225 |
A | PRO227 |
A | HIS263 |
A | ZN401 |
A | ZN402 |
A | HOH1630 |
A | HOH1641 |
A | HOH1673 |
site_id | BC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MP2 B 2410 |
Chain | Residue |
B | TYR33 |
B | TRP39 |
B | ASP120 |
B | PHE156 |
B | GLY161 |
B | HIS196 |
B | SER225 |
B | ZN401 |
B | ZN402 |
B | HOH2508 |
B | HOH2580 |
B | HOH2587 |
B | HOH2590 |
B | HOH2616 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 8 |
Chain | Residue |
A | HOH1655 |
B | ARG276 |
A | PHE248 |
A | ALA249 |
A | ALA300 |
A | ASP301 |
A | GLU304 |
A | HOH1500 |
A | HOH1603 |
A | HOH1633 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 9 |
Chain | Residue |
A | ARG276 |
B | ALA249 |
B | ARG252 |
B | ALA300 |
B | ASP301 |
B | GLU304 |
B | HOH2490 |
B | HOH2577 |
B | HOH2662 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 10 |
Chain | Residue |
A | ARG130 |
A | HOH1480 |
B | ARG148 |
B | ASP152 |
B | ASP171 |
B | ARG172 |
B | ILE173 |
B | HOH2531 |
B | HOH2571 |
B | HOH2677 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 11 |
Chain | Residue |
A | HOH1470 |
B | PRO166 |
B | ALA168 |
B | ASN169 |
B | HOH2536 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 21 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. LlSHaHADhaGPvaelkrrtG |
Chain | Residue | Details |
A | LEU113-GLY133 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS116 | |
B | HIS196 | |
A | HIS118 | |
A | ASP120 | |
A | HIS121 | |
A | HIS196 | |
B | HIS116 | |
B | HIS118 | |
B | ASP120 | |
B | HIS121 | |
Chain | Residue | Details |
A | ASP220 | |
B | ASP220 | |
Chain | Residue | Details |
A | HIS263 | |
B | HIS263 | |
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 | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
A | HIS116 | metal ligand |
A | HIS118 | metal ligand |
A | ASP120 | metal ligand |
A | HIS121 | metal ligand |
A | HIS196 | metal ligand |
A | TYR229 | electrostatic stabiliser, hydrogen bond donor |
A | HIS263 | metal ligand |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 258 |
Chain | Residue | Details |
B | HIS116 | metal ligand |
B | HIS118 | metal ligand |
B | ASP120 | metal ligand |
B | HIS121 | metal ligand |
B | HIS196 | metal ligand |
B | TYR229 | electrostatic stabiliser, hydrogen bond donor |
B | HIS263 | metal ligand |