1NNL
Crystal structure of Human Phosphoserine Phosphatase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001701 | biological_process | in utero embryonic development |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009612 | biological_process | response to mechanical stimulus |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0031667 | biological_process | response to nutrient levels |
| A | 0033574 | biological_process | response to testosterone |
| A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001701 | biological_process | in utero embryonic development |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009612 | biological_process | response to mechanical stimulus |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0031667 | biological_process | response to nutrient levels |
| B | 0033574 | biological_process | response to testosterone |
| B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1500 |
| Chain | Residue |
| A | GLY110 |
| A | LYS158 |
| A | HOH1028 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1502 |
| Chain | Residue |
| B | PHE112 |
| B | SER114 |
| B | LEU135 |
| B | HOH1053 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1503 |
| Chain | Residue |
| A | SER114 |
| A | LEU135 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1505 |
| Chain | Residue |
| A | GLY30 |
| A | GLY111 |
| A | PHE112 |
| A | ILE115 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1506 |
| Chain | Residue |
| B | GLY30 |
| B | GLY111 |
| B | PHE112 |
| B | HOH1072 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1507 |
| Chain | Residue |
| B | GLY110 |
| B | LYS158 |
| B | HOH1068 |
| B | HOH1183 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 2001 |
| Chain | Residue |
| A | ASP20 |
| A | ASP22 |
| A | ASP179 |
| A | HOH1026 |
| A | HOH1028 |
| A | HOH1069 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2002 |
| Chain | Residue |
| B | ASP20 |
| B | ASP22 |
| B | ASP179 |
| B | HOH1021 |
| B | HOH1068 |
| B | HOH1117 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2003 |
| Chain | Residue |
| B | GLU185 |
| B | PRO188 |
| B | HOH1137 |
| B | HOH1222 |
| B | HOH1223 |
| B | HOH1401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J |
| Chain | Residue | Details |
| A | ASP20 | |
| B | ASP20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J |
| Chain | Residue | Details |
| A | ASP22 | |
| B | ASP22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY |
| Chain | Residue | Details |
| A | ASP20 | |
| A | ASP22 | |
| A | ASP179 | |
| B | ASP20 | |
| B | ASP22 | |
| B | ASP179 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J |
| Chain | Residue | Details |
| A | MET52 | |
| B | THR182 | |
| A | GLY53 | |
| A | SER109 | |
| A | LYS158 | |
| A | THR182 | |
| B | MET52 | |
| B | GLY53 | |
| B | SER109 | |
| B | LYS158 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
