2ZXC
Ceramidase complexed with C2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017040 | molecular_function | N-acylsphingosine amidohydrolase activity |
| A | 0042759 | biological_process | long-chain fatty acid biosynthetic process |
| A | 0046512 | biological_process | sphingosine biosynthetic process |
| A | 0046514 | biological_process | ceramide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051872 | biological_process | sphingosine catabolic process |
| A | 0102121 | molecular_function | ceramidase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017040 | molecular_function | N-acylsphingosine amidohydrolase activity |
| B | 0042759 | biological_process | long-chain fatty acid biosynthetic process |
| B | 0046512 | biological_process | sphingosine biosynthetic process |
| B | 0046514 | biological_process | ceramide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051872 | biological_process | sphingosine catabolic process |
| B | 0102121 | molecular_function | ceramidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 647 |
| Chain | Residue |
| A | HIS97 |
| A | HIS204 |
| A | GLU411 |
| A | TYR448 |
| A | HOH686 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 2ED A 701 |
| Chain | Residue |
| A | SER334 |
| A | THR335 |
| A | ASP337 |
| A | GLY338 |
| A | PRO339 |
| A | TYR448 |
| A | TYR460 |
| A | HOH686 |
| A | HOH728 |
| A | TYR26 |
| A | HIS99 |
| A | ARG160 |
| A | HIS204 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 648 |
| Chain | Residue |
| A | PHE67 |
| A | GLN68 |
| A | SER106 |
| A | TYR108 |
| A | ALA444 |
| A | TYR445 |
| A | HOH731 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 649 |
| Chain | Residue |
| A | THR636 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 650 |
| Chain | Residue |
| A | HOH685 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 652 |
| Chain | Residue |
| A | HIS37 |
| A | ASP579 |
| A | ASP581 |
| A | THR584 |
| A | HOH653 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 647 |
| Chain | Residue |
| B | HIS97 |
| B | HIS204 |
| B | GLU411 |
| B | TYR448 |
| B | HOH678 |
| B | 2ED702 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 2ED B 702 |
| Chain | Residue |
| B | GLY25 |
| B | SER27 |
| B | ARG160 |
| B | HIS204 |
| B | THR335 |
| B | ASP337 |
| B | GLY338 |
| B | PRO341 |
| B | TYR448 |
| B | TYR460 |
| B | ZN647 |
| B | HOH678 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 648 |
| Chain | Residue |
| B | PHE67 |
| B | GLN68 |
| B | SER106 |
| B | TYR108 |
| B | ALA444 |
| B | TYR445 |
| B | HOH819 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 650 |
| Chain | Residue |
| B | VAL85 |
| B | ASP87 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT B 651 |
| Chain | Residue |
| B | HOH1057 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS B 652 |
| Chain | Residue |
| B | ARG55 |
| B | TYR82 |
| B | GLN138 |
| B | HOH856 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS B 653 |
| Chain | Residue |
| B | GLU88 |
| B | PHE299 |
| B | SER495 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 654 |
| Chain | Residue |
| B | HIS37 |
| B | ASP579 |
| B | ASP581 |
| B | THR584 |
| B | HOH704 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | SER250 | |
| B | SER250 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19088069, ECO:0007744|PDB:2ZWS, ECO:0007744|PDB:2ZXC |
| Chain | Residue | Details |
| A | HIS37 | |
| B | HIS97 | |
| B | HIS204 | |
| B | GLU411 | |
| B | TYR448 | |
| B | ASP579 | |
| B | ASP581 | |
| B | THR584 | |
| A | HIS97 | |
| A | HIS204 | |
| A | GLU411 | |
| A | TYR448 | |
| A | ASP579 | |
| A | ASP581 | |
| A | THR584 | |
| B | HIS37 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19088069 |
| Chain | Residue | Details |
| A | ASN60 | |
| B | TYR445 | |
| A | GLN68 | |
| A | ASP87 | |
| A | SER106 | |
| A | TYR445 | |
| B | ASN60 | |
| B | GLN68 | |
| B | ASP87 | |
| B | SER106 |
