Structure of PDB 1tzc Chain A

Receptor sequence
>1tzcA (length=301) Species: 178306 (Pyrobaculum aerophilum str. IM2) [Search protein sequence]
SQLLQDYLNWENYILRRVDFPTSYVVEGEVVRIEAMPRLYISGMGGSGVV
ADLIRDFSLTWNWEVEVIAVKDYFLKARDGLLIAVSYSGNTIETLYTVEY
AKRRRIPAVAITTGGRLAQMGVPTVIVPKASAPRAALPQLLTAALHVVAK
VYGIDVKIPEGLEPPNEALIHKLVEEFQKRPTIIAAESMRGVAYRVKNEF
NENAKIEPSVEILPEAHHNWIEGSERAVVALTSPHIPKEHQERVKATVEI
VGGSIYAVEMHPKGVLSFLRDVGIASVKLAEIRGVNPLATPRIDALKRRL
Q
3D structure
PDB1tzc A novel phosphoglucose/phosphomannose isomease from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16 A resolution
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R135 E203 H219 K298
Catalytic site (residue number reindexed from 1) R134 E202 H218 K297
Enzyme Commision number 5.3.1.8: mannose-6-phosphate isomerase.
5.3.1.9: glucose-6-phosphate isomerase.
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 PA5 A G47 S48 S87 Y88 S89 T92 P134 R135 E203 K298 G46 S47 S86 Y87 S88 T91 P133 R134 E202 K297
Gene Ontology
Molecular Function
GO:0004347 glucose-6-phosphate isomerase activity
GO:0004476 mannose-6-phosphate isomerase activity
GO:0016853 isomerase activity
GO:0097367 carbohydrate derivative binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:1901135 carbohydrate derivative metabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1tzc, PDBe:1tzc, PDBj:1tzc
PDBsum1tzc
PubMed15252053
UniProtQ8ZWV0|PGMI_PYRAE Bifunctional phosphoglucose/phosphomannose isomerase (Gene Name=PAE1610)

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