3KXP
Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042820 | biological_process | vitamin B6 catabolic process |
| A | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042820 | biological_process | vitamin B6 catabolic process |
| B | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0042820 | biological_process | vitamin B6 catabolic process |
| C | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0042820 | biological_process | vitamin B6 catabolic process |
| D | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0042820 | biological_process | vitamin B6 catabolic process |
| E | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0042820 | biological_process | vitamin B6 catabolic process |
| F | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0042803 | molecular_function | protein homodimerization activity |
| G | 0042820 | biological_process | vitamin B6 catabolic process |
| G | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0042803 | molecular_function | protein homodimerization activity |
| H | 0042820 | biological_process | vitamin B6 catabolic process |
| H | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0042820 | biological_process | vitamin B6 catabolic process |
| I | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0042803 | molecular_function | protein homodimerization activity |
| J | 0042820 | biological_process | vitamin B6 catabolic process |
| J | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0042803 | molecular_function | protein homodimerization activity |
| K | 0042820 | biological_process | vitamin B6 catabolic process |
| K | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0042803 | molecular_function | protein homodimerization activity |
| L | 0042820 | biological_process | vitamin B6 catabolic process |
| L | 0047411 | molecular_function | 2-(acetamidomethylene)succinate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 279 |
| Chain | Residue |
| A | ILE41 |
| A | SER106 |
| A | LEU107 |
| A | HOH630 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 279 |
| Chain | Residue |
| B | ILE41 |
| B | SER106 |
| B | LEU107 |
| B | HOH455 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 279 |
| Chain | Residue |
| C | SER106 |
| C | LEU107 |
| C | HOH737 |
| C | ILE41 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 279 |
| Chain | Residue |
| D | ILE41 |
| D | SER106 |
| D | LEU107 |
| D | HOH339 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E 279 |
| Chain | Residue |
| E | ILE41 |
| E | SER106 |
| E | LEU107 |
| E | HOH794 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL F 279 |
| Chain | Residue |
| F | ILE41 |
| F | SER106 |
| F | LEU107 |
| F | LEU207 |
| F | HOH432 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL G 279 |
| Chain | Residue |
| G | ILE41 |
| G | SER106 |
| G | LEU107 |
| G | HOH375 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL H 279 |
| Chain | Residue |
| H | ILE41 |
| H | SER106 |
| H | LEU107 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL I 279 |
| Chain | Residue |
| I | ILE41 |
| I | SER106 |
| I | LEU107 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL J 279 |
| Chain | Residue |
| J | ILE41 |
| J | SER106 |
| J | LEU107 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL K 279 |
| Chain | Residue |
| K | ILE41 |
| K | SER106 |
| K | LEU107 |
| K | HOH1381 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL L 279 |
| Chain | Residue |
| L | ILE41 |
| L | SER106 |
| L | LEU107 |
| L | HOH308 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:20099871 |
| Chain | Residue | Details |
| A | SER106 | |
| J | SER106 | |
| K | SER106 | |
| L | SER106 | |
| B | SER106 | |
| C | SER106 | |
| D | SER106 | |
| E | SER106 | |
| F | SER106 | |
| G | SER106 | |
| H | SER106 | |
| I | SER106 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:20099871 |
| Chain | Residue | Details |
| A | ASP130 | |
| E | HIS258 | |
| F | ASP130 | |
| F | HIS258 | |
| G | ASP130 | |
| G | HIS258 | |
| H | ASP130 | |
| H | HIS258 | |
| I | ASP130 | |
| I | HIS258 | |
| J | ASP130 | |
| A | HIS258 | |
| J | HIS258 | |
| K | ASP130 | |
| K | HIS258 | |
| L | ASP130 | |
| L | HIS258 | |
| B | ASP130 | |
| B | HIS258 | |
| C | ASP130 | |
| C | HIS258 | |
| D | ASP130 | |
| D | HIS258 | |
| E | ASP130 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20099871 |
| Chain | Residue | Details |
| A | ILE41 | |
| J | ILE41 | |
| K | ILE41 | |
| L | ILE41 | |
| B | ILE41 | |
| C | ILE41 | |
| D | ILE41 | |
| E | ILE41 | |
| F | ILE41 | |
| G | ILE41 | |
| H | ILE41 | |
| I | ILE41 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER106 | |
| J | SER106 | |
| K | SER106 | |
| L | SER106 | |
| B | SER106 | |
| C | SER106 | |
| D | SER106 | |
| E | SER106 | |
| F | SER106 | |
| G | SER106 | |
| H | SER106 | |
| I | SER106 |
