Structure of PDB 4rpk Chain A

Receptor sequence
>4rpkA (length=392) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TARFDLFVVGSGFFGLTIAERVATQLDKRVLVLERRPHIGGNAYSEAEPQ
TGIEVHKYGAHLFHTSNKRVWDYVRQFTDFTDYRHRVFAMHNGQAYQFPM
GLGLVSQFFGKYFTPEQARQLIAEQAAEIDTADAQNLEEKAISLIGRPLY
EAFVKGYTAKQWQTDPKELPAANITRLPVRYTFDNRYFSDTYEGLPTDGY
TAWLQNMAADHRIEVRLNTDWFDVRGQLRPGSPAAPVVYTGPLDRYFDYA
EGRLGWRTLDFEVEVLPIGDFQGTAVMNYNDLDVPYTRIHEFRHFHPERD
YRTDKTVIMREYSRFAEDDDEPYYPINTEADRALLATYRARAKSETASSK
VLFGGRLGTYQYLDMHMAIASALNMYDNVLAPHLRDGVPLLQ
3D structure
PDB4rpk Structural Basis of Ligand Binding to UDP-Galactopyranose Mutase from Mycobacterium tuberculosis Using Substrate and Tetrafluorinated Substrate Analogues.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R180 R184 R261 R292 E315 Y366 D368
Catalytic site (residue number reindexed from 1) R176 R180 R257 R288 E311 Y362 D364
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4rpk, PDBe:4rpk, PDBj:4rpk
PDBsum4rpk
PubMed25562380
UniProtP9WIQ1|GLF_MYCTU UDP-galactopyranose mutase (Gene Name=glf)

[Back to BioLiP]