Structure of PDB 4qtf Chain A

Receptor sequence
>4qtfA (length=349) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
VPKLTASVTDGAVGVTVDAPVSVTAADGVLAAVTMVNDNGRPVAGRLSPD
GLRWSTTEQLGYNRRYTLNATALGLGGAATRQLTFQTSSPAHLTMPYVMP
GDGEVVGVGEPVAIRFDENIADRGAAEKAIKITTNPPVEGAFYWLNNREV
RWRPEHFWKPGTAVDVAVNTYGVDLGEGMFGEDNVQTHFTIGDEVIATAD
DNTKILTVRVNGEVVKSMPTSMGKDSTPTANGIYIVGSRYKHIIMDSSTY
GVPVNSPNGYRTDVDWATQISYSGVFVHSAPWSVGAQGHTNTSHGCLNVS
PSNAQWFYDHVKRGDIVEVVNTVGGTLPGIDGLGDWNIPWDQWRAGNAK
3D structure
PDB4qtf Structure and specificity of L-D-Transpeptidase from Mycobacterium tuberculosis and antibiotic resistance: Calcium binding promotes dimer formation
ChainA
Resolution2.0 Å
3D
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
Enzyme Commision number 2.3.2.-
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 MLD A L62 T63 A64 S65 R139 L4 T5 A6 S7 R81
BS02 3V5 A M303 G332 H336 H352 G353 C354 M245 G274 H278 H294 G295 C296
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
GO:0071972 peptidoglycan L,D-transpeptidase activity
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0018104 peptidoglycan-protein cross-linking
GO:0071555 cell wall organization
Cellular Component
GO:0005886 plasma membrane

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4qtf, PDBe:4qtf, PDBj:4qtf
PDBsum4qtf
PubMed
UniProtI6Y9J2|LDT2_MYCTU L,D-transpeptidase 2 (Gene Name=ldtB)

[Back to BioLiP]