Structure of PDB 1o98 Chain A

Receptor sequence
>1o98A (length=509) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
SKKPVALIILDGFALRDETYGNAVAQANKPNFDRYWNEYPHTTLKACGEA
VGLPEGQMGNSEVGHLNIGAGRIVYQSLTRINIAIREGEFDRNETFLAAM
NHVKQHGTSLHLFGLLSDGGVHSHIHHLYALLRLAAKEGVKRVYIHGFLD
GRDVGPQTAPQYIKELQEKIKEYGVGEIATLSGRYYSMDRDKRWDRVEKA
YRAMVYGEGPTYRDPLECIEDSYKHGIYDEFVLPSVIVREDGRPVATIQD
NDAIIFYNFRPDRAIQISNTFTNEDFREFDRGPKHPKHLFFVCLTHFSET
VAGYVAFKPTNLDNTIGEVLSQHGLRQLRIAETEKYPHVTFFMSGGREEE
FPGEDRILINSPKVPTYDLKPEMSAYEVTDALLKEIEADKYDAIILNYAN
PDMVGHSGKLEPTIKAVEAVDECLGKVVDAILAKGGIAIITADHGNADEV
LTPDGKPQTAHTTNPVPVIVTKKGIKLRDGGILGDLAPTMLDLLGLPQPK
EMTGKSLIV
3D structure
PDB1o98 Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase from X-Ray Crystallography, Simulated Dynamics and Molecular Modeling
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D12 S62 D154 R261 K336 D403 H407 D444 H445 H462
Catalytic site (residue number reindexed from 1) D11 S61 D153 R260 K335 D402 H406 D443 H444 H461
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 MN A D403 H407 H462 D402 H406 H461
BS02 MN A D12 S62 D444 H445 D11 S61 D443 H444
BS03 2PG A S62 H123 R153 D154 R185 R191 R261 R264 K336 D403 H462 S61 H122 R152 D153 R184 R190 R260 R263 K335 D402 H461
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
GO:0030435 sporulation resulting in formation of a cellular spore
GO:0043937 regulation of sporulation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1o98, PDBe:1o98, PDBj:1o98
PDBsum1o98
PubMed12729763
UniProtQ9X519|GPMI_GEOSE 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (Gene Name=gpmI)

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