4FLR
Crystal structure of Amylosucrase double mutant A289P-F290L from Neisseria polysaccharea
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS A 701 |
| Chain | Residue |
| A | ASP144 |
| A | HOH875 |
| A | TYR147 |
| A | HIS187 |
| A | PHE250 |
| A | ASP286 |
| A | GLU328 |
| A | ARG509 |
| A | GOL708 |
| A | GOL717 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | ASP403 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | HIS332 |
| A | PHE399 |
| A | ASP401 |
| A | GLU402 |
| A | ARG415 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | GLU328 |
| A | ILE330 |
| A | TYR349 |
| A | TYR388 |
| A | SER391 |
| A | HIS392 |
| A | ASP393 |
| A | GOL717 |
| A | HOH1000 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 705 |
| Chain | Residue |
| A | ARG86 |
| A | GLU87 |
| A | PRO90 |
| A | ARG317 |
| A | PRO321 |
| A | PHE324 |
| A | GOL706 |
| A | HOH835 |
| A | HOH921 |
| A | HOH922 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 706 |
| Chain | Residue |
| A | PRO90 |
| A | ARG317 |
| A | PHE324 |
| A | GLN342 |
| A | GLN346 |
| A | HIS382 |
| A | GOL705 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 707 |
| Chain | Residue |
| A | ASP91 |
| A | LEU94 |
| A | SER95 |
| A | ASP552 |
| A | GLY553 |
| A | HOH964 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL A 708 |
| Chain | Residue |
| A | TYR104 |
| A | MET133 |
| A | ASP144 |
| A | GLY145 |
| A | TYR147 |
| A | HIS392 |
| A | ASP393 |
| A | ARG509 |
| A | ARG513 |
| A | TRS701 |
| A | HOH875 |
| A | HOH1004 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 709 |
| Chain | Residue |
| A | GLY396 |
| A | TRP397 |
| A | THR398 |
| A | ASP444 |
| A | CYS445 |
| A | ARG446 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 710 |
| Chain | Residue |
| A | ARG226 |
| A | ILE228 |
| A | GLU328 |
| A | ALA329 |
| A | ILE330 |
| A | GOL717 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 711 |
| Chain | Residue |
| A | PHE229 |
| A | GLN232 |
| A | ASN251 |
| A | GLN437 |
| A | ASP506 |
| A | ASP507 |
| A | ARG509 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 712 |
| Chain | Residue |
| A | TYR51 |
| A | ASN54 |
| A | SER260 |
| A | ASN562 |
| A | THR589 |
| A | THR592 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 713 |
| Chain | Residue |
| A | ILE93 |
| A | LEU94 |
| A | SER95 |
| A | GLY480 |
| A | LEU481 |
| A | ARG545 |
| A | PHE551 |
| A | GLY553 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 714 |
| Chain | Residue |
| A | LYS564 |
| A | ILE566 |
| A | HOH993 |
| A | HOH994 |
| A | HOH1012 |
| A | GLU55 |
| A | VAL366 |
| A | PHE559 |
| A | ASN560 |
| A | THR561 |
| A | ASN563 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 715 |
| Chain | Residue |
| A | ASN424 |
| A | PHE426 |
| A | ASP427 |
| A | GLY428 |
| A | SER429 |
| A | HOH1035 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 716 |
| Chain | Residue |
| A | ASN207 |
| A | ASN258 |
| A | SER260 |
| A | HIS591 |
| A | GLN594 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 717 |
| Chain | Residue |
| A | PHE229 |
| A | GLU328 |
| A | ASP393 |
| A | ASP394 |
| A | PHE436 |
| A | ARG446 |
| A | TRS701 |
| A | GOL704 |
| A | GOL710 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 718 |
| Chain | Residue |
| A | TRP194 |
| A | GLU271 |
| A | 1PE720 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 719 |
| Chain | Residue |
| A | ASP202 |
| A | PRO203 |
| A | ASP526 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE A 720 |
| Chain | Residue |
| A | LEU204 |
| A | PHE205 |
| A | PHE208 |
| A | TRP263 |
| A | ARG266 |
| A | ALA267 |
| A | GOL718 |
| A | HOH879 |
| A | HOH1013 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15023061","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10828446","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10828446","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11467966","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12364331","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15023061","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






