Structure of PDB 5kgn Chain B

Receptor sequence
>5kgnB (length=521) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
MAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQ
IEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTN
ESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPEL
YLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDN
RWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGE
KGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGM
TQYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFN
GGLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFI
MCNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADH
GNAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTV
LAIMGLPQPAEMTGVSIVQKI
3D structure
PDB5kgn Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D37 S86 D178 R284 K359 D426 H430 D467 H468 H485
Catalytic site (residue number reindexed from 1) D19 S68 D160 R266 K341 D408 H412 D449 H450 H467
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 B L82 N85 E87 V88 Q101 D102 R284 D286 R289 T319 P333 F366 L64 N67 E69 V70 Q83 D84 R266 D268 R271 T301 P315 F348
BS02 MG B I50 L51 A53 T55 I32 L33 A35 T37
BS03 MN B D426 H430 H485 D408 H412 H467
BS04 ZN B D37 S86 D467 H468 D19 S68 D449 H450
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:5kgn, PDBe:5kgn, PDBj:5kgn
PDBsum5kgn
PubMed28368002
UniProtG5EFZ1|GPMI_CAEEL 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=ipgm-1)

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