Structure of PDB 2adv Chain C

Receptor sequence

>2advC (length=494) Species: 405038 (Pseudomonas sp. GK16)

DYFTLYEAHLVTPDFEIYGATQIGLPVIRFAFNQRMGITNTVNGMVGATN
YRLTLQDGGYLYDGQVRPFERRQASYRLRQADGTTVDKPLEIRSSVHGPV
FERADGTAVAVRVAGLDRPGMLEQYFDMITADSFDDYEAALARMQVPTFN
IVYADREGTINYSFNGVAPKRAEGDIAFWQGLVPGDSSRYLWTETHPLDD
LPRVTNPPGGFVQNSNDPPWTPTWPVTYTPKDFPSYLAPQTPHSLRAQQS
VRLMSENDDLTLERFMALQLSHRAVMADRTLPDLIPAALIDPDPEVQAAA
RLLAAWDREFTSDSRAALLFEEWARLFAGQNFAGQAGFATPWSLDKPVST
PYGVRDPKAAVDQLRTAIANTKRKYGAIDRPFGDASRMILNDVNVPGAAG
YGNLGSFRVFTWSDPDENGVRTPVHGETWVAMIEFSTPVRAYGLMSYGNS
RQPGTTHYSDQIERVSRADFRELLLRREQVEAAVQERTPFNFKP

3D structure

• PDB: 2adv Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
• Chain: C
• Resolution: 2.244 Å

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.

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	peptide	C	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	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

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity

Biological Process

• GO:0017000 antibiotic biosynthetic process

External links

• PDB: RCSB:2adv, PDBe:2adv, PDBj:2adv
• PDBsum: 2adv
• PubMed: 16446446
• UniProt: P07662|G7AC_PSEU7 Glutaryl-7-aminocephalosporanic-acid acylase