1SNZ
Crystal structure of apo human galactose mutarotase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004034 | molecular_function | aldose 1-epimerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006012 | biological_process | galactose metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019318 | biological_process | hexose metabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004034 | molecular_function | aldose 1-epimerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006012 | biological_process | galactose metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019318 | biological_process | hexose metabolic process |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0033499 | biological_process | galactose catabolic process via UDP-galactose, Leloir pathway |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
| site_id | PS00545 |
| Number of Residues | 10 |
| Details | ALDOSE_1_EPIMERASE Aldose 1-epimerase putative active site. NlTNHsYFNL |
| Chain | Residue | Details |
| A | ASN172-LEU181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15026423","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15026423","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15026423","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SO0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66HG4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| A | HIS176 | |
| A | GLU307 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details |
| Chain | Residue | Details |
| B | HIS176 | |
| B | GLU307 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 351 |
| Chain | Residue | Details |
| A | HIS107 | electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS176 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU307 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 351 |
| Chain | Residue | Details |
| B | HIS107 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS176 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU307 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
