Structure of PDB 6u0z Chain A

Receptor sequence
>6u0zA (length=266) Species: 522373 (Stenotrophomonas maltophilia K279a) [Search protein sequence]
EAPLPQLRAYTVDASWLQPMAPLQVADHTWQIGTEDLTALLVQTAEGAVL
LDGGMPQMAGHLLDNMKLRGVAPQDLRLILLSHAHADHAGPVAELKRRTG
AHVAANAETAVLLARGGSNDLHFGDGITYPPASADRIIMDGEVVTVGGIA
FTAHFMPGHTPGSTAWTWTDTRDGKPVRIAYADSLSAPGYQLKGNPRYPR
LIEDYKRSFATVRALPCDLLLTPHPGASNWNYAVGSKASAEALTCNAYAD
AAEKKFDAQLARETAG
3D structure
PDB6u0z Crystal Structure of the metallo-beta-lactamase L1 from Stenotrophomonas maltophilia in the complex with the hydrolyzed penicillin G.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H105 H107 D109 H110 H181 Y212 H246
Catalytic site (residue number reindexed from 1) H83 H85 D87 H88 H159 Y190 H224
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 GLC A N251 W252 N253 N229 W230 N231
BS02 FRU A E57 D58 G248 W252 N253 Y254 A255 E35 D36 G226 W230 N231 Y232 A233
BS03 FRU A R200 C239 R178 C217
BS04 PNK A Y32 H107 D109 F145 H181 S206 S208 P210 H246 Y10 H85 D87 F123 H159 S184 S186 P188 H224
BS05 ZN A H105 H107 H181 H83 H85 H159
BS06 ZN A D109 H110 H246 D87 H88 H224
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
Biological Process
GO:0017001 antibiotic catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6u0z, PDBe:6u0z, PDBj:6u0z
PDBsum6u0z
PubMed
UniProtB2FTM1

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