Structure of PDB 4bl3 Chain B

Receptor sequence
>4bl3B (length=639) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
KDKEINNTIDAIEDKNFKQVYKDSSYISKSDNGEVEMTERPIKIYNSLGV
KDINIQDRKIKKVSKNKKRVDAQYKIKTNYGNIDRNVQFNFVKEDGMWKL
DWDHSVIIPGMQKDQSIHIEKLKSERGKILDRNNVELANTGTAYEIGIVP
KNVSKKDYKAIAKELSISEDYIKQQMDQNWVQDDTFVPLKTVKKMDEYLS
DFAKKFHLTTNETESRNYPLGKATSHLLGYVGPINSEELKQKEYKGYKDD
AVIGKKGLEKLYDKKLQHEDGYRVTIVDDNSNTIAHTLIEKKKKDGKDIQ
LTIDAKVQKSIYNNMKNDYGSGTAIHPQTGELLALVSTPSYDVYPFMYGM
SNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLDDKTSY
KIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELG
SKKFEKGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEIL
INPVQILSIYSALENNGNINAPHLLKDTKNKVWKKNIISKENINLLTDGM
QQVVNKTHKEDIYRSYANLIGKSGTAELKMKGRQIGWFISYDKDNPNMMM
AINVKDVQDKGMASYNAKISGKVYDELYENGNKKYDIDE
3D structure
PDB4bl3 Disruption of Allosteric Response as an Unprecedented Mechanism of Resistance to Antibiotics.
ChainB
Resolution3.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase.
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 MUR B E150 R151 N164 T165 S240 R241 V277 H293 E125 R126 N139 T140 S215 R216 V252 H268
Gene Ontology
Molecular Function
GO:0008658 penicillin binding
GO:0071972 peptidoglycan L,D-transpeptidase activity
Biological Process
GO:0046677 response to antibiotic
GO:0071555 cell wall organization
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4bl3, PDBe:4bl3, PDBj:4bl3
PDBsum4bl3
PubMed24955778
UniProtA0A0H3JPA5

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