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PDBsum entry 2z02
Go to PDB code:
Ligase
PDB id
2z02
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Contents
Protein chains
242 a.a.
*
Ligands
SO4
×3
ATP
×2
CIT
Waters
×299
*
Residue conservation analysis
PDB id:
2z02
Links
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RCSB
MMDB
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CATH
SCOP
PDBSWS
PDBePISA
PROCOGNATE
ProSAT
Name:
Ligase
Title:
Crystal structure of phosphoribosylaminoimidazolesuccinocarboxamide synthase wit atp from methanocaldococcus jannaschii
Structure:
Phosphoribosylaminoimidazole-succinocarboxamide synthase. Chain: a, b. Synonym: saicar synthetase. Engineered: yes
Source:
Methanocaldococcus jannaschii. Organism_taxid: 2190. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.03Å
R-factor:
0.207
R-free:
0.217
Authors:
M.Kanagawa,S.Baba,S.Kuramitsu,S.Yokoyama,G.Kawai,G.Sampei,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref:
M.Kanagawa et al. Crystal structure of phosphoribosylaminoimidazolesuccinocarboxamide synthase from methanocaldococcus jannaschii.
To be published
, .
Date:
06-May-07
Release date:
06-Nov-07
PROCHECK
Headers
References
Protein chains
?
Q58987
(PUR7_METJA) - Phosphoribosylaminoimidazole-succinocarboxamide synthase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Seq:
Struc:
242 a.a.
242 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.6.3.2.6
- phosphoribosylaminoimidazolesuccinocarboxamide synthase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Pathway:
Purine Biosynthesis (late stages)
Reaction:
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamido]succinate + ADP + phosphate + 2 H
+
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
+
L-aspartate
Bound ligand (Het Group name =
ATP
)
corresponds exactly
+
ATP
Bound ligand (Het Group name =
CIT
)
matches with 57.14% similarity
=
(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamido]succinate
+
ADP
+
phosphate
+
2 × H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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