2Z9W
Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047300 | molecular_function | pyridoxamine-pyruvate transaminase activity |
| B | 0004760 | molecular_function | L-serine-pyruvate transaminase activity |
| B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019265 | biological_process | glycine biosynthetic process, by transamination of glyoxylate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047300 | molecular_function | pyridoxamine-pyruvate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1601 |
| Chain | Residue |
| A | GLY17 |
| A | TYR95 |
| A | ARG336 |
| A | ARG345 |
| A | HOH1611 |
| A | HOH1940 |
| A | HOH1952 |
| B | GOL957 |
| B | HOH2653 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1603 |
| Chain | Residue |
| A | LYS219 |
| A | ARG226 |
| A | HOH1636 |
| A | HOH1810 |
| A | HOH1868 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1605 |
| Chain | Residue |
| A | PRO23 |
| A | GLU24 |
| A | ARG27 |
| A | ARG31 |
| A | THR32 |
| A | HOH1883 |
| A | HOH1987 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2601 |
| Chain | Residue |
| A | GOL958 |
| A | HOH1622 |
| A | HOH1730 |
| B | GLY17 |
| B | TYR95 |
| B | ARG336 |
| B | ARG345 |
| B | HOH2629 |
| B | HOH2873 |
| B | HOH2919 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2602 |
| Chain | Residue |
| B | PRO5 |
| B | GLU6 |
| B | HIS7 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2604 |
| Chain | Residue |
| B | ARG310 |
| B | PRO312 |
| B | ASP313 |
| B | ARG374 |
| B | HOH2674 |
| B | HOH2714 |
| B | HOH2827 |
| B | HOH2960 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2605 |
| Chain | Residue |
| A | ASP9 |
| B | PRO23 |
| B | GLU24 |
| B | ARG27 |
| B | ARG31 |
| B | THR32 |
| B | HOH2918 |
| B | HOH2954 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXL A 1197 |
| Chain | Residue |
| A | GLU68 |
| A | PRO69 |
| A | TYR95 |
| A | HIS144 |
| A | THR146 |
| A | ASP171 |
| A | VAL173 |
| A | SER174 |
| A | ASN196 |
| A | LYS197 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PXL B 1197 |
| Chain | Residue |
| B | GLU68 |
| B | PRO69 |
| B | TYR95 |
| B | HIS144 |
| B | THR146 |
| B | ASP171 |
| B | VAL173 |
| B | SER174 |
| B | ASN196 |
| B | LYS197 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 953 |
| Chain | Residue |
| A | SER298 |
| A | ASP299 |
| A | SER300 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 954 |
| Chain | Residue |
| B | SER298 |
| B | ASP299 |
| B | SER300 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 955 |
| Chain | Residue |
| A | GLY98 |
| A | TRP102 |
| A | HOH1657 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 956 |
| Chain | Residue |
| B | GLY98 |
| B | TYR101 |
| B | TRP102 |
| B | HOH2767 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 957 |
| Chain | Residue |
| A | ARG336 |
| A | SO41601 |
| B | ASP36 |
| B | TYR37 |
| B | PHE245 |
| B | THR248 |
| B | HOH2916 |
| B | HOH2965 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 958 |
| Chain | Residue |
| A | ASP36 |
| A | TYR37 |
| A | PHE245 |
| A | THR248 |
| A | HOH1652 |
| A | HOH1918 |
| B | ARG336 |
| B | SO42601 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 960 |
| Chain | Residue |
| A | HOH1958 |
| B | ILE12 |
| B | THR13 |
| B | ASN20 |
| B | PRO351 |
| B | TYR357 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17989071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"17989071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR95 | |
| A | ASP171 | |
| A | LYS217 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR95 | |
| B | ASP171 | |
| B | LYS217 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR95 | |
| A | LYS197 | |
| A | ASP171 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR95 | |
| B | LYS197 | |
| B | ASP171 |
