Structure of PDB 2h5a Chain X

Receptor sequence
>2h5aX (length=455) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
LPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGR
LSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGS
HNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPR
YFKQIRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDG
NFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTII
YPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGH
SLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQR
DSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDG
VRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSS
LPVPF
3D structure
PDB2h5a Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
ChainX
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H109 D242 D244 D246 R247 D340
Catalytic site (residue number reindexed from 1) H101 D234 D236 D238 R239 D332
Enzyme Commision number 5.4.2.2: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
5.4.2.8: phosphomannomutase.
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 ZN X S108 D242 D244 D246 S100 D234 D236 D238
BS02 X1P X Y17 T306 G307 H308 E325 S327 H329 R421 S423 N424 T425 Y9 T298 G299 H300 E317 S319 H321 R413 S415 N416 T417 PDBbind-CN: -logKd/Ki=5.10,Kd=8uM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004614 phosphoglucomutase activity
GO:0004615 phosphomannomutase activity
GO:0016853 isomerase activity
GO:0016868 intramolecular phosphotransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process
GO:0009244 lipopolysaccharide core region biosynthetic process
GO:0009298 GDP-mannose biosynthetic process
GO:0042121 alginic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2h5a, PDBe:2h5a, PDBj:2h5a
PDBsum2h5a
PubMed16880541
UniProtP26276|ALGC_PSEAE Phosphomannomutase/phosphoglucomutase (Gene Name=algC)

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