Structure of PDB 3igz Chain B Binding Site BS03

Receptor Information
>3igz Chain B (length=549) Species: 5665 (Leishmania mexicana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LLLKPHKDLPRRTVLIVVMDGLGIGPEDDYDAVHMASTPFMDAHRRDNRH
FRCVRAHGTAVGLPTDADMGNSEVGHNALGAGRVALQGASLVDDAIKSGE
IYTGEGYRYLHGAFSKEGSTLHLIGLLSDGGVHSRDNQIYSIIEHAVKDG
AKRIRVHALYDGRDVPDGSSFRFTDELEAVLAKVRQNGCDAAIASGGGRM
FVTMDRYDADWSIVERGWRAQVLGDARHFHSAKEAITTFREEDPKVTDQY
YPPFIVVDEQDKPLGTIEDGDAVLCVNFRGDRVIEMTRAFEDEDFNKFDR
VRVPKVRYAGMMRYDGDLGIPNNFLVPPPKLTRVSEEYLCGSGLNIFACS
ETQKFGHVTYFWNGNRSGKIDEKHETFKEVPSDRVQFNEKPRMQSAAITE
AAIEALKSGMYNVVRINFPNGDMVGHTGDLKATITGVEAVDESLAKLKDA
VDSVNGVYIVTADHGNSDDMAQRDKKGKPMKDGNGNVLPLTSHTLSPVPV
FIGGAGLDPRVAMRTDLPAAGLANVTATFINLLGFEAPEDYEPSLIYVE
Ligand information
Ligand ID2PG
InChIInChI=1S/C3H7O7P/c4-1-2(3(5)6)10-11(7,8)9/h2,4H,1H2,(H,5,6)(H2,7,8,9)/t2-/m1/s1
InChIKeyGXIURPTVHJPJLF-UWTATZPHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(C(=O)O)OP(=O)(O)O)O
ACDLabs 10.04O=P(O)(O)OC(C(=O)O)CO
OpenEye OEToolkits 1.5.0C([C@H](C(=O)O)OP(=O)(O)O)O
CACTVS 3.341OC[C@@H](O[P](O)(O)=O)C(O)=O
CACTVS 3.341OC[CH](O[P](O)(O)=O)C(O)=O
FormulaC3 H7 O7 P
Name2-PHOSPHOGLYCERIC ACID
ChEMBL
DrugBankDB01709
ZINCZINC000003869232
PDB chain3igz Chain B Residue 565 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3igz Crystal structures of Leishmania mexicana phosphoglycerate mutase suggest a one-metal mechanism and a new enzyme subclass
Resolution1.9 Å
Binding residue
(original residue number in PDB)		S75 H136 D167 R202 R209 R282 R285 K357 D425 H429 H496
Binding residue
(residue number reindexed from 1)		S72 H133 D164 R199 R206 R279 R282 K354 D422 H426 H493
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D23 R282 K357 D425 H429 D466 H467 H496
Catalytic site (residue number reindexed from 1) D20 R279 K354 D422 H426 D463 H464 H493
Enzyme Commision number 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
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: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:3igz, PDBe:3igz, PDBj:3igz
PDBsum3igz
PubMed19781556
UniProtQ86N96

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