Structure of PDB 4rpj Chain A

Receptor sequence
>4rpjA (length=393) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MTARFDLFVVGSGFFGLTIAERVATQLDKRVLVLERRPHIGGNAYSEAEP
QTGIEVHKYGAHLFHTSNKRVWDYVRQFTDFTDYRHRVFAMHNGQAYQFP
MGLGLVSQFFGKYFTPEQARQLIAEQAAEIDTADAQNLEEKAISLIGRPL
YEAFVKGYTAKQWQTDPKELPAANITRLPVRYTFDNRYFSDTYEGLPTDG
YTAWLQNMAADHRIEVRLNTDWFDVRGQLRPGSPAAPVVYTGPLDRYFDY
AEGRLGWRTLDFEVEVLPIGDFQGTAVMNYNDLDVPYTRIHEFRHFHPER
DYRTDKTVIMREYSRFAEDDDEPYYPINTEADRALLATYRARAKSETASS
KVLFGGRLGTYQYLDMHMAIASALNMYDNVLAPHLRDGVPLLQ
3D structure
PDB4rpj Structural Basis of Ligand Binding to UDP-Galactopyranose Mutase from Mycobacterium tuberculosis Using Substrate and Tetrafluorinated Substrate Analogues.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R180 R184 R261 R292 E315 Y366 D368
Catalytic site (residue number reindexed from 1) R177 R181 R258 R289 E312 Y363 D365
Enzyme Commision number 5.4.99.9: UDP-galactopyranose mutase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0008767 UDP-galactopyranose mutase activity
GO:0016853 isomerase activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0045227 capsule polysaccharide biosynthetic process
GO:0071555 cell wall organization
GO:0071766 Actinobacterium-type cell wall biogenesis
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4rpj, PDBe:4rpj, PDBj:4rpj
PDBsum4rpj
PubMed25562380
UniProtP9WIQ1|GLF_MYCTU UDP-galactopyranose mutase (Gene Name=glf)

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