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5OLY

5-fluorotryptophan labeled beta-phosphoglucomutase in a closed conformation, monoclinic crystal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0008801molecular_functionbeta-phosphoglucomutase activity
A0016853molecular_functionisomerase activity
A0046872molecular_functionmetal ion binding
G0000287molecular_functionmagnesium ion binding
G0005737cellular_componentcytoplasm
G0005975biological_processcarbohydrate metabolic process
G0008801molecular_functionbeta-phosphoglucomutase activity
G0016853molecular_functionisomerase activity
G0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12081483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LVH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 206
ChainResidueDetails
AASP8metal ligand, nucleofuge, nucleophile
AGLY174metal ligand
ALEU9electrostatic stabiliser, hydrogen bond donor
AASP10metal ligand, proton acceptor, proton donor
ATHR16electrostatic stabiliser
AARG49electrostatic stabiliser
AASN118electrostatic stabiliser, hydrogen bond donor
AGLY119electrostatic stabiliser, hydrogen bond donor
AASP149electrostatic stabiliser, hydrogen bond donor
AALA173metal ligand

site_idMCSA2
Number of Residues10
DetailsM-CSA 206
ChainResidueDetails

246905

PDB entries from 2025-12-31

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