4BKM
Crystal structure of the murine AUM (phosphoglycolate phosphatase) capping domain as a fusion protein with the catalytic core domain of murine chronophin (pyridoxal phosphate phosphatase)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1304 |
| Chain | Residue |
| A | ASP25 |
| A | ASP27 |
| A | ASP247 |
| A | ASP252 |
| A | HOH2004 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1304 |
| Chain | Residue |
| B | ASP25 |
| B | ASP27 |
| B | ASP247 |
| B | HOH2003 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 1304 |
| Chain | Residue |
| C | ASP25 |
| C | ASP27 |
| C | ASP247 |
| C | HOH2004 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 1304 |
| Chain | Residue |
| D | ASP25 |
| D | ASP27 |
| D | ASP247 |
| D | HOH2004 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1305 |
| Chain | Residue |
| A | ASN59 |
| A | SER61 |
| A | ARG62 |
| A | PHE159 |
| A | ASN186 |
| A | THR202 |
| A | HOH2036 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1306 |
| Chain | Residue |
| A | ARG197 |
| A | PHE198 |
| A | HOH2042 |
| A | HOH2056 |
| B | GLN176 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:24338687, ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES |
| Chain | Residue | Details |
| A | ASP25 | |
| B | ASP25 | |
| C | ASP25 | |
| D | ASP25 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24338687, ECO:0000305|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES |
| Chain | Residue | Details |
| A | ASP27 | |
| B | ASP27 | |
| C | ASP27 | |
| D | ASP27 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BKM, ECO:0007744|PDB:4BX0, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:4BX3, ECO:0007744|PDB:5AES |
| Chain | Residue | Details |
| A | ASP25 | |
| D | ASP25 | |
| D | ASP27 | |
| D | ASP247 | |
| A | ASP27 | |
| A | ASP247 | |
| B | ASP25 | |
| B | ASP27 | |
| B | ASP247 | |
| C | ASP25 | |
| C | ASP27 | |
| C | ASP247 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190, ECO:0007744|PDB:4BX2, ECO:0007744|PDB:5AES |
| Chain | Residue | Details |
| A | SER58 | |
| A | LYS222 | |
| B | SER58 | |
| B | LYS222 | |
| C | SER58 | |
| C | LYS222 | |
| D | SER58 | |
| D | LYS222 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Important for substrate specificity => ECO:0000305|PubMed:24338473 |
| Chain | Residue | Details |
| A | LEU191 | |
| B | LEU191 | |
| C | LEU191 | |
| D | LEU191 |
