Structure of PDB 1jvz Chain B

Receptor sequence
>1jvzB (length=520) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
SNSWAVAPGKTANGNALLLQNPHLSWTTDYFTYYEAHLVTPDFEIYGATQ
IGLPVIRFAFNQRMGITNTVNGMVGATNYRLTLQDGGYLYDGQVRPFERR
QASYRLRQADGSTVDKPLEIRSSVHGPVFERADGTAVAVRVAGLDRPGML
EQYFDMITAHSFDDYEAAMARMQVPTFNIVYADREGTINYSFNGVAPKRA
EGDIAFWQGNVPGDSSRYLWTETHPLDDLPRVTNPPGGFVQNSNDPPWTP
TWPVTYCPANHPSYLAPQTPHSLRAQQSVRLMSENDDLTLERFMALQFSH
RAVMADRTLPDLIPAALIDPDPEVQAAARLLAAWDRDFTSDSRAALLFEE
WARLFAGQNFAGQAAFATPWSLDKPVSTPYGVRDPKAAVDQLRTAIANTK
RKYGAIDRPFGDASRMILNDVNVPGAAGYGNLGSFRVFTWSDPDENGIRT
PVHGETWVAMIEFSTPVRAYGLMSYGNSRQPGTTHYSDQIERVSRADFRE
LLLRREQVEAAVQERTPFNF
3D structure
PDB1jvz Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S170 H192 V239 N413 E624
Catalytic site (residue number reindexed from 1) S1 H23 V70 N244 E455
Enzyme Commision number 3.5.1.93: glutaryl-7-aminocephalosporanic-acid acylase.
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 CEN B S170 H192 L193 Y202 R226 F227 V239 S1 H23 L24 Y33 R57 F58 V70
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1jvz, PDBe:1jvz, PDBj:1jvz
PDBsum1jvz
PubMed11755403
UniProtQ9L5D6|G7AC_BREDI Glutaryl-7-aminocephalosporanic-acid acylase

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