Structure of PDB 7tl7 Chain D

Receptor sequence
>7tl7D (length=521) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
AMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQI
EAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNE
SLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELY
LHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNR
WERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEK
GRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMT
QYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNG
GLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIM
CNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHG
NAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVL
AIMGLPQPAEMTGVSIVQKIK
3D structure
PDB7tl7 Serum-Stable and Selective Backbone-N-Methylated Cyclic Peptides That Inhibit Prokaryotic Glycolytic Mutases.
ChainD
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide D P79 N85 E87 Q101 V146 H147 R284 D286 F366 H485 P60 N66 E68 Q82 V127 H128 R265 D267 F347 H466
BS02 ZN D D426 H430 H485 D407 H411 H466
BS03 ZN D D37 S86 D467 H468 D18 S67 D448 H449
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004619 phosphoglycerate mutase activity
GO:0016853 isomerase activity
GO:0030145 manganese ion binding
GO:0046537 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006007 glucose catabolic process
GO:0006096 glycolytic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7tl7, PDBe:7tl7, PDBj:7tl7
PDBsum7tl7
PubMed35904259
UniProtG5EFZ1|GPMI_CAEEL 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=ipgm-1)

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