Structure of PDB 6fm0 Chain B

Receptor sequence
>6fm0B (length=290) Species: 1076759 (Vibrio phage phiVC8) [Search protein sequence]
ENVDLVIDLQFGSTGKGLIAGYLAEKNGYDTVINANMPNAGHTYINAEGR
KWMHKVLPNGIVSPNLKRVMLGAGSVFSINRLMEEIEMSKDLLHDKVAIL
IHPMATVLDGSMAAMVEKLQRDPTNNTIVARDVAQYDGRIAQYVCTVEEW
DMALMASERILAEGAQGFSLSLNQEFYPYCTSRDCTPARFLADMGIPLPM
LNKVIGTARCHPIRVGHYPDQEERRVFSFSFIQMQKAMWTCQPDEVFLNF
CNYLSPQDIVHQIEVAAQSRYCDAEVKYLGFGPTFNDVEL
3D structure
PDB6fm0 A third purine biosynthetic pathway encoded by aminoadenine-based viral DNA genomes.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S14 K17 G42 H43 Q187
Catalytic site (residue number reindexed from 1) S13 K16 G41 H42 Q166
Enzyme Commision number 6.3.4.25: 2-amino-2'-deoxyadenylo-succinate synthase.
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 ATP B S14 G16 K17 H43 T44 F295 G330 P331 S13 G15 K16 H42 T43 F250 G282 P283
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004019 adenylosuccinate synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
GO:0046040 IMP metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6fm0, PDBe:6fm0, PDBj:6fm0
PDBsum6fm0
PubMed33926955
UniProtG3FFN6|PURZ_BPVC8 N6-succino-2-amino-2'-deoxyadenylate synthase (Gene Name=purZ)

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