Structure of PDB 5kgn Chain A

Receptor sequence
>5kgnA (length=530) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
AMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQI
EAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNE
SLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELY
LHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNR
WERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEK
GRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMT
QYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNG
GLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIM
CNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHG
NAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVL
AIMGLPQPAEMTGVSIVQKIKLAAALEHHH
3D structure
PDB5kgn Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) D18 S67 D159 R265 K340 D407 H411 D448 H449 H466
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 A L82 N85 E87 Q101 D102 R284 D286 R289 T319 P333 F366 L63 N66 E68 Q82 D83 R265 D267 R270 T300 P314 F347
BS02 MG A I50 L51 A53 T55 I31 L32 A34 T36
BS03 MN A D426 H430 H485 D407 H411 H466
BS04 ZN A 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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
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)

[Back to BioLiP]