Structure of PDB 2adv Chain C Binding Site BS01

Receptor Information
>2adv Chain C (length=494) Species: 405038 (Pseudomonas sp. GK16) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DYFTLYEAHLVTPDFEIYGATQIGLPVIRFAFNQRMGITNTVNGMVGATN
YRLTLQDGGYLYDGQVRPFERRQASYRLRQADGTTVDKPLEIRSSVHGPV
FERADGTAVAVRVAGLDRPGMLEQYFDMITADSFDDYEAALARMQVPTFN
IVYADREGTINYSFNGVAPKRAEGDIAFWQGLVPGDSSRYLWTETHPLDD
LPRVTNPPGGFVQNSNDPPWTPTWPVTYTPKDFPSYLAPQTPHSLRAQQS
VRLMSENDDLTLERFMALQLSHRAVMADRTLPDLIPAALIDPDPEVQAAA
RLLAAWDREFTSDSRAALLFEEWARLFAGQNFAGQAGFATPWSLDKPVST
PYGVRDPKAAVDQLRTAIANTKRKYGAIDRPFGDASRMILNDVNVPGAAG
YGNLGSFRVFTWSDPDENGVRTPVHGETWVAMIEFSTPVRAYGLMSYGNS
RQPGTTHYSDQIERVSRADFRELLLRREQVEAAVQERTPFNFKP
Ligand information
>2adv Chain B (length=28) Species: 405038 (Pseudomonas sp. GK16) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
SNSWAVAPGKTANGNALLLQNPHLSWTT
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2adv Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Resolution2.244 Å
Binding residue
(original residue number in PDB)
L33 F58 A59 G65 T67 T69 G186 G238 F239 V240 Q241 N242 S243 N244 R274 S278 M282 N285 D287 L288 F293 Q297 F435 V437 P451 V452 H453 G454 E455 W457 V458 A459 M460 I461 E462 F463 S464 S474 R479
Binding residue
(residue number reindexed from 1)
L5 F30 A31 G37 T39 T41 G158 G210 F211 V212 Q213 N214 S215 N216 R246 S250 M254 N257 D259 L260 F265 Q269 F407 V409 P423 V424 H425 G426 E427 W429 V430 A431 M432 I433 E434 F435 S436 S446 R451
Enzymatic activity
Catalytic site (original residue number in PDB) V70 N244 E455
Catalytic site (residue number reindexed from 1) V42 N216 E427
Enzyme Commision number 3.5.1.93: glutaryl-7-aminocephalosporanic-acid acylase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2adv, PDBe:2adv, PDBj:2adv
PDBsum2adv
PubMed16446446
UniProtP07662|G7AC_PSEU7 Glutaryl-7-aminocephalosporanic-acid acylase

[Back to BioLiP]