Structure of PDB 1bls Chain B Binding Site BS01

Receptor Information
>1bls Chain B (length=359) Species: 550 (Enterobacter cloacae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAAN
KPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQW
QGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYA
NASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAW
GYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQG
IALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEV
NPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVE
AAYHILEAL
Ligand information
Ligand IDIPP
InChIInChI=1S/C9H11INO3P/c10-8-3-1-7(2-4-8)5-9(12)11-6-15(13)14/h1-4,15H,5-6H2,(H,11,12)(H,13,14)
InChIKeyNJMHQBSYSLWOQF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1CC(=O)NC[P@H](=O)O)I
CACTVS 3.341O[P@@H](=O)CNC(=O)Cc1ccc(I)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1CC(=O)NCP(=O)O)I
CACTVS 3.341O[PH](=O)CNC(=O)Cc1ccc(I)cc1
ACDLabs 10.04Ic1ccc(cc1)CC(=O)NCP(=O)O
FormulaC9 H11 I N O3 P
Name(P-IODOPHENYLACETYLAMINO)METHYLPHOSPHINIC ACID
ChEMBL
DrugBankDB04123
ZINCZINC000003870423
PDB chain1bls Chain B Residue 362 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1bls Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		S64 Y150 Y221 G317 S318
Binding residue
(residue number reindexed from 1)		S63 Y149 Y220 G316 S317
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 V121 Y150 G156 E272 K315 S318
Catalytic site (residue number reindexed from 1) S63 K66 Y111 V120 Y149 G155 E271 K314 S317
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1bls, PDBe:1bls, PDBj:1bls
PDBsum1bls
PubMed8204611
UniProtP05364|AMPC_ENTCL Beta-lactamase (Gene Name=ampC)

[Back to BioLiP]