1JTP
Degenerate interfaces in antigen-antibody complexes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| L | 0003796 | molecular_function | lysozyme activity |
| L | 0003824 | molecular_function | catalytic activity |
| L | 0005539 | molecular_function | glycosaminoglycan binding |
| L | 0005576 | cellular_component | extracellular region |
| L | 0005615 | cellular_component | extracellular space |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| L | 0016998 | biological_process | cell wall macromolecule catabolic process |
| L | 0031640 | biological_process | killing of cells of another organism |
| L | 0042742 | biological_process | defense response to bacterium |
| L | 0042802 | molecular_function | identical protein binding |
| L | 0050829 | biological_process | defense response to Gram-negative bacterium |
| L | 0050830 | biological_process | defense response to Gram-positive bacterium |
| M | 0003796 | molecular_function | lysozyme activity |
| M | 0003824 | molecular_function | catalytic activity |
| M | 0005539 | molecular_function | glycosaminoglycan binding |
| M | 0005576 | cellular_component | extracellular region |
| M | 0005615 | cellular_component | extracellular space |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0016787 | molecular_function | hydrolase activity |
| M | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| M | 0016998 | biological_process | cell wall macromolecule catabolic process |
| M | 0031640 | biological_process | killing of cells of another organism |
| M | 0042742 | biological_process | defense response to bacterium |
| M | 0042802 | molecular_function | identical protein binding |
| M | 0050829 | biological_process | defense response to Gram-negative bacterium |
| M | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | ASP99 |
| A | THR101 |
| A | GLY119 |
| A | ASP121 |
| A | HOH510 |
| A | HOH537 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 502 |
| Chain | Residue |
| B | ASP121 |
| B | HOH511 |
| M | HOH559 |
| B | ASP99 |
| B | THR101 |
| B | GLY119 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA L 503 |
| Chain | Residue |
| L | SER60 |
| L | CYS64 |
| L | SER72 |
| L | LYS73 |
| L | HOH515 |
| L | HOH568 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA M 504 |
| Chain | Residue |
| M | SER60 |
| M | CYS64 |
| M | SER72 |
| M | LYS73 |
| M | HOH520 |
| M | HOH533 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA L 505 |
| Chain | Residue |
| A | SER105 |
| L | GLU35 |
| L | FMT406 |
| L | HOH526 |
| L | HOH550 |
| L | HOH551 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 401 |
| Chain | Residue |
| A | ALA6 |
| A | TYR94 |
| A | TYR95 |
| A | CYS96 |
| A | GLY124 |
| A | GLY126 |
| A | THR127 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FMT B 402 |
| Chain | Residue |
| B | ALA6 |
| B | TYR94 |
| B | TYR95 |
| B | CYS96 |
| B | GLY124 |
| B | GLN125 |
| B | GLY126 |
| B | THR127 |
| B | HOH566 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT M 403 |
| Chain | Residue |
| M | ASN65 |
| M | GLY67 |
| M | ARG68 |
| M | THR69 |
| M | SER72 |
| M | HOH520 |
| M | HOH533 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT M 404 |
| Chain | Residue |
| B | HOH511 |
| M | HOH543 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT M 405 |
| Chain | Residue |
| L | ASN113 |
| L | ARG114 |
| L | HOH540 |
| M | ARG5 |
| M | CYS6 |
| M | HOH511 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT L 406 |
| Chain | Residue |
| L | GLU35 |
| L | VAL109 |
| L | ALA110 |
| L | NA505 |
| L | HOH551 |
| L | HOH571 |
| L | HOH576 |
Functional Information from PROSITE/UniProt
| site_id | PS00128 |
| Number of Residues | 19 |
| Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC |
| Chain | Residue | Details |
| L | CYS76-CYS94 |
| site_id | PS00879 |
| Number of Residues | 17 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gkereg.VaAINMGGGIT |
| Chain | Residue | Details |
| A | GLY42-THR58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 256 |
| Details | Domain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 132l |
| Chain | Residue | Details |
| L | GLU35 | |
| L | ASP52 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 132l |
| Chain | Residue | Details |
| M | GLU35 | |
| M | ASP52 |
