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5OK0

Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis trapped with native reaction intermediate beta-glucose 1,6-bisphosphate to 2.2A resolution.

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP8

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AASN10

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP8
AASP170
AASN10
ATRP24
ALEU44
ASER52
ALYS76
ASER114
ALYS145
AGLU169

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups
ChainResidueDetails
ASER114
ALYS145

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095
ChainResidueDetails
AASP8

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 206
ChainResidueDetails
AASP8metal ligand, nucleofuge, nucleophile
AASP170metal ligand
ALEU9electrostatic stabiliser, hydrogen bond donor
AASN10metal ligand, proton acceptor, proton donor
ATHR16electrostatic stabiliser
ALYS45electrostatic stabiliser
ASER114electrostatic stabiliser, hydrogen bond donor
AALA115electrostatic stabiliser, hydrogen bond donor
ALYS145electrostatic stabiliser, hydrogen bond donor
AGLU169metal ligand

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PDB entries from 2024-04-24

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