1VKL
RABBIT MUSCLE PHOSPHOGLUCOMUTASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004614 | molecular_function | phosphoglucomutase 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 | 0016529 | cellular_component | sarcoplasmic reticulum |
A | 0016853 | molecular_function | isomerase activity |
A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004614 | molecular_function | phosphoglucomutase 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 | 0016529 | cellular_component | sarcoplasmic reticulum |
B | 0016853 | molecular_function | isomerase activity |
B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI A 562 |
Chain | Residue |
A | ASP287 |
A | ASP289 |
A | ASP291 |
A | SEP116 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI B 562 |
Chain | Residue |
B | SEP116 |
B | ASP287 |
B | ASP289 |
B | ASP291 |
B | HOH706 |
site_id | MBA |
Number of Residues | 4 |
Details | METAL ATOM IN 562. |
Chain | Residue |
A | ASP287 |
A | ASP289 |
A | ASP291 |
A | SEP116 |
site_id | MBB |
Number of Residues | 4 |
Details | METAL ATOM IN 562. |
Chain | Residue |
B | ASP287 |
B | ASP289 |
B | ASP291 |
B | SEP116 |
Functional Information from PROSITE/UniProt
site_id | PS00710 |
Number of Residues | 10 |
Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GIiLTASHNP |
Chain | Residue | Details |
A | GLY110-PRO119 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PubMed","id":"5669853","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-1999","submissionDatabase":"PDB data bank","title":"Binding driven structural changes in crystaline phosphoglucomutase associated with chemical reaction.","authors":["Baranidharan S.","Ray W.J. Jr.","Liu Y."]}},{"source":"PDB","id":"1C47","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"description":"via phosphate group","evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15299905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PMG","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 10 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P38652","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9D0F9","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by PAK1","evidences":[{"source":"UniProtKB","id":"P36871","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 352 |
Chain | Residue | Details |
A | SEP116 | activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLY121 | proton acceptor, proton donor |
A | ASP291 | metal ligand |
A | ASN293 | metal ligand |
A | ILE295 | metal ligand |
A | LEU296 | electrostatic stabiliser |
A | TRP392 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 352 |
Chain | Residue | Details |
B | SEP116 | activator, covalently attached, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
B | GLY121 | proton acceptor, proton donor |
B | ASP291 | metal ligand |
B | ASN293 | metal ligand |
B | ILE295 | metal ligand |
B | LEU296 | electrostatic stabiliser |
B | TRP392 | proton acceptor, proton donor |