Structure of PDB 4rl0 Chain B Binding Site BS04

Receptor Information
>4rl0 Chain B (length=239) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVR
DGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDA
LHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLK
VFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAA
SARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR
Ligand information
Ligand ID3S0
InChIInChI=1S/C16H18N4O9S/c1-27-20-10(8-3-2-4-28-8)12(21)18-11(15(24)25)13-19-9(14(22)23)7(6-30-13)5-29-16(17)26/h2-4,7,11,13H,5-6H2,1H3,(H2,17,26)(H,18,21)(H,22,23)(H,24,25)/b20-10-/t7-,11-,13+/m0/s1
InChIKeyAYUIRPIPSPPXAA-NEHUYCMOSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)C(NC(=O)C(=N\OC)/c1occc1)C2N=C(C(=O)O)C(COC(=O)N)CS2
CACTVS 3.385CO\N=C(/C(=O)N[C@@H]([C@H]1SC[C@H](COC(N)=O)C(=N1)C(O)=O)C(O)=O)c2occc2
CACTVS 3.385CON=C(C(=O)N[CH]([CH]1SC[CH](COC(N)=O)C(=N1)C(O)=O)C(O)=O)c2occc2
OpenEye OEToolkits 1.7.6CON=C(c1ccco1)C(=O)NC(C2N=C(C(CS2)COC(=O)N)C(=O)O)C(=O)O
OpenEye OEToolkits 1.7.6CO/N=C(/c1ccco1)\C(=O)N[C@@H]([C@@H]2N=C([C@H](CS2)COC(=O)N)C(=O)O)C(=O)O
FormulaC16 H18 N4 O9 S
Name(2R,5S)-5-[(carbamoyloxy)methyl]-2-[(R)-carboxy{[(2Z)-2-(furan-2-yl)-2-(methoxyimino)acetyl]amino}methyl]-5,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
ChEMBL
DrugBank
ZINCZINC000219058912
PDB chain4rl0 Chain B Residue 303 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4rl0 Structural and Mechanistic Insights into NDM-1 Catalyzed Hydrolysis of Cephalosporins.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		I35 W93 H122 Q123 D124 H189 C208 K211 N220 H250
Binding residue
(residue number reindexed from 1)		I4 W62 H91 Q92 D93 H158 C177 K180 N189 H219
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H120 H122 D124 H189 C208 K211 N220 H250
Catalytic site (residue number reindexed from 1) H89 H91 D93 H158 C177 K180 N189 H219
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4rl0, PDBe:4rl0, PDBj:4rl0
PDBsum4rl0
PubMed25268575
UniProtC7C422|BLAN1_KLEPN Metallo-beta-lactamase type 2 (Gene Name=blaNDM-1)

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