1S1D
Structure and protein design of human apyrase
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | SER98 |
| A | ASP99 |
| A | GLU145 |
| A | GLU214 |
| A | SER275 |
| A | GLU326 |
| A | HOH5158 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1002 |
| Chain | Residue |
| B | GLU214 |
| B | SER275 |
| B | GLU326 |
| B | HOH5041 |
| B | SER98 |
| B | GLU145 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 2001 |
| Chain | Residue |
| A | ASP133 |
| A | LYS143 |
| A | ASN172 |
| A | ASN174 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| Chain | Residue |
| B | LYS60 |
| B | HIS81 |
| B | TYR325 |
| B | HOH5314 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3002 |
| Chain | Residue |
| B | ARG113 |
| B | LYS143 |
| B | TRP163 |
| B | TRS5006 |
| B | HOH5216 |
| B | HOH5269 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GP2 A 4001 |
| Chain | Residue |
| A | ASP42 |
| A | ASP44 |
| A | ASP112 |
| A | GLU145 |
| A | LYS161 |
| A | GLU162 |
| A | TRP163 |
| A | THR164 |
| A | TYR237 |
| A | ASP242 |
| A | LYS324 |
| A | GLU326 |
| A | HOH5169 |
| A | HOH5275 |
| A | HOH5309 |
| A | HOH5336 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GP2 B 4002 |
| Chain | Residue |
| B | ASP42 |
| B | ASP44 |
| B | LYS161 |
| B | GLU162 |
| B | TRP163 |
| B | THR164 |
| B | GLU214 |
| B | ARG230 |
| B | TYR237 |
| B | ASP242 |
| B | GLU295 |
| B | LYS324 |
| B | GLU326 |
| B | HOH5055 |
| B | HOH5083 |
| B | HOH5140 |
| B | HOH5157 |
| B | HOH5322 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS A 5001 |
| Chain | Residue |
| A | TYR21 |
| A | VAL102 |
| A | VAL149 |
| A | LYS278 |
| A | GLU329 |
| A | HOH5025 |
| A | HOH5026 |
| A | HOH5044 |
| A | HOH5091 |
| A | HOH5207 |
| A | HOH5295 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TRS A 5002 |
| Chain | Residue |
| A | LEU23 |
| A | LEU59 |
| A | LYS61 |
| A | LEU107 |
| A | ILE120 |
| A | GLU121 |
| A | GLY122 |
| A | ILE331 |
| A | TRS5007 |
| A | HOH5108 |
| A | HOH5142 |
| B | TYR63 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS B 5003 |
| Chain | Residue |
| B | TYR21 |
| B | GLU329 |
| B | HOH5017 |
| B | HOH5019 |
| B | HOH5068 |
| B | HOH5070 |
| B | HOH5196 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS B 5004 |
| Chain | Residue |
| B | ILE331 |
| B | HOH5132 |
| B | HOH5144 |
| A | TYR63 |
| A | TRS5007 |
| B | LEU23 |
| B | LEU59 |
| B | LYS61 |
| B | LEU107 |
| B | ILE120 |
| B | GLY122 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS A 5005 |
| Chain | Residue |
| A | ILE260 |
| A | ALA261 |
| A | VAL262 |
| A | HOH5102 |
| A | HOH5298 |
| A | HOH5312 |
| B | ALA232 |
| B | SER233 |
| B | GLN234 |
| B | LYS245 |
| B | HOH5089 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TRS B 5006 |
| Chain | Residue |
| B | ASP133 |
| B | LYS140 |
| B | LYS143 |
| B | TRP163 |
| B | ASN172 |
| B | ASN174 |
| B | PRO175 |
| B | SO43002 |
| B | HOH5020 |
| B | HOH5128 |
| B | HOH5134 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS A 5007 |
| Chain | Residue |
| A | ARG36 |
| A | LYS61 |
| A | TRS5002 |
| A | HOH5256 |
| B | ARG36 |
| B | LYS61 |
| B | TRS5004 |
| B | HOH5185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15006348","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16835225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S18","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S1D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H2N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H2U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15006348","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16835225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S18","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H2N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2H2U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Important for dimer formation","evidences":[{"source":"PubMed","id":"16835225","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
