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7KNF

1.80A resolution structure of independent Phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (Ce-1 NHOH)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006007biological_processglucose catabolic process
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0030145molecular_functionmanganese ion binding
A0046537molecular_function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006007biological_processglucose catabolic process
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0030145molecular_functionmanganese ion binding
B0046537molecular_function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9X519
ChainResidueDetails
BSER86
ASER86

site_idSWS_FT_FI2
Number of Residues26
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9X519
ChainResidueDetails
AASP426
AHIS430
AASP467
AHIS468
AHIS485
BASP37
BSER86
BHIS147
BARG177
BARG210
BARG216
BARG284
BLYS359
BASP426
BHIS430
BASP467
BHIS468
BHIS485
AARG210
AARG216
AARG284
ALYS359
AASP37
ASER86
AHIS147
AARG177

221051

PDB entries from 2024-06-12

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