Structure of PDB 1gk0 Chain B

Receptor sequence
>1gk0B (length=522) Species: 306 (Pseudomonas sp.) [Search protein sequence]
SNSWAVAPGKTANGNALLLQNPHLSWTTDYFTYYEAHLVTPDFEIYGATQ
IGLPVIRFAFNQRMGITNTVNGMVGATNYRLTLQDGGYLYDGQVRPFERR
QASYRLRQADGTTVDKPLEIRSSVHGPVFERADGTAVAVRVAGLDRPGML
EQYFDMITADSFDDYEAALARMQVPTFNIVYADREGTINYSFNGVAPKRA
EGDIAFWQGLVPGDSSRYLWTETHPLDDLPRVTNPPGGFVQNSNDPPWTP
TWPVTYTPKDFPSYLAPQTPHSLRAQQSVRLMSENDDLTLERFMALQLSH
RAVMADRTLPDLIPAALIDPDPEVQAAARLLAAWDREFTSDSRAALLFEE
WARLFAGQNFAGQAGFATPWSLDKPVSTPYGVRDPKAAVDQLRTAIANTK
RKYGAIDRPFGDASRMILNDVNVPGAAGYGNLGSFRVFTWSDPDENGVRT
PVHGETWVAMIEFSTPVRAYGLMSYGNSRQPGTTHYSDQIERVSRADFRE
LLLRREQVEAAVQERTPFNFKP
3D structure
PDB1gk0 Structure-Based Prediction of Modifications in Glutarylamidase to Allow Single-Step Enzymatic Production of 7-Aminocephalosporanic Acid from Cephalosporin C.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S1 H23 V70 N244 E455
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 PO4 B S1 H23 V70 N244 S1 H23 V70 N244
BS02 EDO B R57 T69 F177 R57 T69 F177
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:1gk0, PDBe:1gk0, PDBj:1gk0
PDBsum1gk0
PubMed11742126
UniProtP07662|G7AC_PSEU7 Glutaryl-7-aminocephalosporanic-acid acylase

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