Structure of PDB 4zad Chain B

Receptor sequence
>4zadB (length=510) Species: 42374 (Candida dubliniensis) [Search protein sequence]
LNPALKFRDFIQVLKNEGDLIEIDTEVDPNLEVGAITRKAYENKLAAPLF
NNLKQDPENIDPKNLFRILGCPGGLRGFGNDHARIALHLGLDSQTPMKEI
IDFLVANRNPKKYIPPVLVPNDQSPHKKHHLTKEQIDLTKLPVPLLHHGD
GGKFIQTYGMWVLQTPDKSWTNWSIARGMVHDSKSITGLVINPQHVKQVS
DAWVAAGKGDKIPFALCFGVPPAAILVSSMPIPDGATEAEYIGGLCNQAV
PVVKCETNDLEVPADCEMVFEGYLDRDTLVREGPFGEMHGYCFPKDHHTQ
PLYRVNHISYRDQAIMPISNPGLCTDETHTLIGGLVSAETKYLISQHPVL
SKIVEDVFTPYEAQALWLAVKINTHELVKLKTNAKELSNLVGDFLFRSKE
CYKVCSILHEIILVGDDIDIFDFKQLIWAYTTRHTPVQDQLYFDDVKPFA
LAPFASQGPLIKTRQGGKCVTTCIFPKQFTDPDFEFVTCNFNGYPEEVNK
ISQNWDKYYK
3D structure
PDB4zad New cofactor supports alpha , beta-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition.
ChainB
Resolution2.46 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 4.1.1.102: phenacrylate decarboxylase.
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 MN B N174 H197 E240 N172 H195 E238
BS02 4LU B T159 N174 S176 I177 R179 Q196 H197 S231 M232 P233 S321 I334 K404 T157 N172 S174 I175 R177 Q194 H195 S229 M230 P231 S319 I332 K403
Gene Ontology
Molecular Function
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0033494 ferulate metabolic process
GO:0046281 cinnamic acid catabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4zad, PDBe:4zad, PDBj:4zad
PDBsum4zad
PubMed26083754
UniProtB9WJ66|FDC1_CANDC Ferulic acid decarboxylase 1 (Gene Name=FDC1)

[Back to BioLiP]