Structure of PDB 1s6r Chain A

Receptor sequence
>1s6rA (length=359) Species: 550 (Enterobacter cloacae) [Search protein sequence]
VSEKQLAEVVANTVTPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANK
PVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDPVTRYWPQLTGKQWQ
GIRMLDLATYTAGGLPLQVPDEVTDNASLVRFYQNWQPQWKPGTTRLYAN
ASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWG
YRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGI
ALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVVEVN
PPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEA
AYHILEALQ
3D structure
PDB1s6r Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue.
ChainA
Resolution2.24 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) S64 K67 Y112 V121 Y150 G156 E272 K315 S318
Catalytic site (residue number reindexed from 1) S62 K65 Y110 V119 Y148 G154 E270 K313 S316
Enzyme Commision number 3.5.2.6: beta-lactamase.
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 IAP A S64 Q120 Y150 N152 Y221 S318 S62 Q118 Y148 N150 Y219 S316
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1s6r, PDBe:1s6r, PDBj:1s6r
PDBsum1s6r
PubMed14521155
UniProtQ93CA2

[Back to BioLiP]