Structure of PDB 4c5s Chain C

Receptor sequence
>4c5sC (length=642) Species: 29808 (Taxus chinensis) [Search protein sequence]
SHVKDILGLINAFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAECR
ARVETCSSWVQRKAEDGADIAGVTTGFGACSSRRTNRLSELQESLIRCLL
AGVFTDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPK
VPLRGSVSGDLIPLAYIAGLLIGKPSVIARIGDDVEVPAPEALSRVGLRP
FKLQAKEGLALVNGTSFATAVASTVMYDANVLLLLVETLCGMFCEVIFGR
EEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQELSREYYSIDKLKKPK
QDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHG
ANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGP
DLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALIS
ARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADEC
GLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLKQSCFDTILALHE
TDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKVRIQGSKFLPFYRFVREE
LDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFL
3D structure
PDB4c5s Structural Investigations Into the Stereochemistry and Activity of a Phenylalanine-2,3-Aminomutase from Taxus Chinensis.
ChainC
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) A80 G87 L108 N231 Y322 R325 F371 Q459
Catalytic site (residue number reindexed from 1) A71 G78 L99 N213 Y304 R307 F353 Q441
Enzyme Commision number 4.3.1.24: phenylalanine ammonia-lyase.
5.4.3.10: phenylalanine aminomutase (L-beta-phenylalanine forming).
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 BQ7 C G87 X175 L179 N231 N355 F371 E455 G78 X159 L161 N213 N337 F353 E437
BS02 BQ7 C Y322 R325 Y304 R307
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016841 ammonia-lyase activity
GO:0016853 isomerase activity
GO:0016869 intramolecular aminotransferase activity
GO:0045548 phenylalanine ammonia-lyase activity
Biological Process
GO:0006558 L-phenylalanine metabolic process
GO:0006559 L-phenylalanine catabolic process
GO:0009698 phenylpropanoid metabolic process
GO:0009800 cinnamic acid biosynthetic process
GO:0009820 alkaloid metabolic process
GO:0009821 alkaloid biosynthetic process
GO:0042617 paclitaxel biosynthetic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4c5s, PDBe:4c5s, PDBj:4c5s
PDBsum4c5s
PubMed24786474
UniProtQ68G84|PAM_TAXCH Phenylalanine aminomutase (L-beta-phenylalanine forming) (Gene Name=pam)

[Back to BioLiP]