Structure of PDB 1jl0 Chain B

Receptor sequence

>1jl0B (length=311) Species: 9606 (Homo sapiens)

HFFEGTEKLLEVWFSRQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSF
FYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLY
TLDFRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLI
PGSVIDATMFNPCGYSMNGMKSDGTYWTIAITPEPEFSYVSFETNLSQTS
YDDLIRKVVEVFKPGKFVTTLFVNQSSKCPQKIEGFKRLDCQSAMFNDYN
FVFTSFAKKQQ

3D structure

• PDB: 1jl0 Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant.
• Chain: B
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E67 S68 C82 S229 A243
• Catalytic site (residue number reindexed from 1): E57 S58 C72 S216 A230
• Enzyme Commision number: 4.1.1.50: adenosylmethionine 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	PUT	B	E15 F111 D174 T176 F285 Y318	E11 F101 D161 T163 F272 Y299

Gene Ontology

Molecular Function

• GO:0004014 adenosylmethionine decarboxylase activity
• GO:0005515 protein binding
• GO:0016831 carboxy-lyase activity
• GO:0019810 putrescine binding
• GO:0042802 identical protein binding

Biological Process

• GO:0006595 polyamine metabolic process
• GO:0006597 spermine biosynthetic process
• GO:0008295 spermidine biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1jl0, PDBe:1jl0, PDBj:1jl0
• PDBsum: 1jl0
• PubMed: 11583148
• UniProt: P17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)