Structure of PDB 1jl0 Chain B Binding Site BS01

Receptor Information
>1jl0 Chain B (length=311) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HFFEGTEKLLEVWFSRQGSGDLRTIPRSEWDILLKDVQCSIISVTKTDKQ
EAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSF
FYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAGYCMGRMNSDCWYLY
TLDFRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLI
PGSVIDATMFNPCGYSMNGMKSDGTYWTIAITPEPEFSYVSFETNLSQTS
YDDLIRKVVEVFKPGKFVTTLFVNQSSKCPQKIEGFKRLDCQSAMFNDYN
FVFTSFAKKQQ
Ligand information
Ligand IDPUT
InChIInChI=1S/C4H12N2/c5-3-1-2-4-6/h1-6H2
InChIKeyKIDHWZJUCRJVML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CCN)CN
ACDLabs 10.04
CACTVS 3.341		NCCCCN
FormulaC4 H12 N2
Name1,4-DIAMINOBUTANE;
PUTRESCINE
ChEMBLCHEMBL46257
DrugBankDB01917
ZINCZINC000005828633
PDB chain1jl0 Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1jl0 Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		E15 F111 D174 T176 F285 Y318
Binding residue
(residue number reindexed from 1)		E11 F101 D161 T163 F272 Y299
Annotation score1
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.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jl0, PDBe:1jl0, PDBj:1jl0
PDBsum1jl0
PubMed11583148
UniProtP17707|DCAM_HUMAN S-adenosylmethionine decarboxylase proenzyme (Gene Name=AMD1)

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