Structure of PDB 4nmn Chain A

Receptor sequence
>4nmnA (length=425) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
PCDESAERAVLGSMLEDPENIPLVLEYLKEEDFCIDEHKLLFRVLTNLWS
EYGNKLDFVLIKDHLEKKNLLQIDWLEELYEEAVSPDTLEEVCKIVKQRS
AQRAIIQLGIELIHKGKENKDFHTLIEEAQSRIFSIAESSTQFYHVKDVA
EEVIELIYKFKSSDRLVTGLPSGFTELDLKTTGFHPGDLIILAARPGMGK
TAFMLSIIYNLAKDEGKPSAVFSLEMSKEQLVMRLLSMMSEVPLFKIRSG
SISNEDLKKLEASAIELAKYDIYLDDTPALTTTDLRIRARKLRKEKEVEF
VAVDYLQLLRPPVRKSPRQEEVAEVSRNLKALAKELRIPVMALAQLSREV
EKRSDKRPQLADLRESGQIEQDADLILFLHRPEYYTKKPNEQGIAEVIIA
KQRQGPTDIVKLAFIKEYTKFANLE
3D structure
PDB4nmn Nucleotide and partner-protein control of bacterial replicative helicase structure and function.
ChainA
Resolution3.301 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.4.12: DNA helicase.
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 ADP A G209 G211 K212 T213 R246 L256 R393 F428 T433 G197 G199 K200 T201 R234 L244 R381 F414 T419
BS02 MG A T213 E237 T201 E225
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003678 DNA helicase activity
GO:0004386 helicase activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
Biological Process
GO:0006260 DNA replication
GO:0006268 DNA unwinding involved in DNA replication
GO:0006269 DNA replication, synthesis of primer
GO:0032508 DNA duplex unwinding
Cellular Component
GO:0005829 cytosol
GO:1990077 primosome complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4nmn, PDBe:4nmn, PDBj:4nmn
PDBsum4nmn
PubMed24373746
UniProtO67450

[Back to BioLiP]