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PDBsum entry 3maf
Go to PDB code:
Lyase
PDB id
3maf
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Contents
Protein chains
441 a.a.
*
395 a.a.
*
Ligands
PO4
Metals
_CL
Waters
×126
*
Residue conservation analysis
PDB id:
3maf
Links
PDBe
RCSB
MMDB
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Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Lyase
Title:
Crystal structure of stspl (asymmetric form)
Structure:
Sphingosine-1-phosphate lyase. Chain: a. Engineered: yes. Other_details: llp at residue 311. Sphingosine-1-phosphate lyase. Chain: b. Engineered: yes
Source:
Symbiobacterium thermophilum. Organism_taxid: 2734. Gene: sth1274. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.97Å
R-factor:
0.203
R-free:
0.265
Authors:
F.Bourquin,M.G.Grutter,G.Capitani
Key ref:
F.Bourquin et al. (2010). Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism.
Structure
,
18
, 1054-1065.
PubMed id:
20696404
Date:
23-Mar-10
Release date:
18-Aug-10
PROCHECK
Headers
References
Protein chain
?
Q67PY4
(Q67PY4_SYMTH) - Putative sphingosine-1-phosphate lyase from Symbiobacterium thermophilum (strain T / IAM 14863)
Seq:
Struc:
507 a.a.
441 a.a.
*
Protein chain
?
Q67PY4
(Q67PY4_SYMTH) - Putative sphingosine-1-phosphate lyase from Symbiobacterium thermophilum (strain T / IAM 14863)
Seq:
Struc:
507 a.a.
395 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
Chains A, B:
E.C.4.1.2.27
- sphinganine-1-phosphate aldolase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
sphinganine 1-phosphate = hexadecanal + phosphoethanolamine
sphinganine 1-phosphate
=
hexadecanal
+
phosphoethanolamine
Bound ligand (Het Group name =
PO4
)
matches with 62.50% similarity
Cofactor:
Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
reference
Structure
18
:1054-1065 (2010)
PubMed id:
20696404
Structure and function of sphingosine-1-phosphate lyase, a key enzyme of sphingolipid metabolism.
F.Bourquin,
H.Riezman,
G.Capitani,
M.G.Grütter.
ABSTRACT
No abstract given.
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