Structure of PDB 1m2x Chain C

Receptor sequence
>1m2xC (length=217) Species: 238 (Elizabethkingia meningoseptica) [Search protein sequence]
DVKIEKLKDNLYVYTTYNTFNGTKYAANAVYLVTDKGVVVIDCPWGEDKF
KSFTDEIYKKHGKKVIMNIATHSHDDRAGGLEYFGKIGAKTYSTKMTDSI
LAKENKPRAQYTFDNNKSFKVGKSEFQVYYPGKGHTADNVVVWFPKEKVL
VGGCIIKSADSKDLGYIGEAYVNDWTQSVHNIQQKFSGAQYVVAGHDDWK
DQRSIQHTLDLINEYQQ
3D structure
PDB1m2x The 1.5 A structure of Chryseobacterium meningosepticum Zn-beta-lactamase in complex with the inhibitor, D-captopril
ChainC
Resolution1.5 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) H116 H118 D120 H196 C221 K224 Y233 H263
Catalytic site (residue number reindexed from 1) H72 H74 D76 H135 C154 K157 Y166 H196
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 ZN C H116 H118 H196 H72 H74 H135
BS02 ZN C D120 C221 H263 D76 C154 H196
BS03 ZN C H285 D288 H207 D210
BS04 MCO C H118 D119 D120 K167 H196 Y233 H74 D75 D76 K106 H135 Y166 MOAD: Ki~85uM
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1m2x, PDBe:1m2x, PDBj:1m2x
PDBsum1m2x
PubMed12684522
UniProtO08498|BLAB1_ELIME Metallo-beta-lactamase type 2 (Gene Name=blaB1)

[Back to BioLiP]