Structure of PDB 3dsr Chain A

Receptor sequence
>3dsrA (length=419) Species: 2209 (Methanosarcina mazei) [Search protein sequence]
AGPLIFVEKTEPVGYNEIVNIKMGDGTVRRGQVLDSSADIVVVQVFEGIF
TGETLKLPASVDLLGRILSGSGEPRDGGPRIVPDQLLDINGAAMNPYARL
PPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPHNEIALQIARQASVPG
SESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADDPAVERI
VTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGAPGYMYTDLAT
LYERAGIVKGAKGSVTQIPILSMPPIPDLSGYITEGQIVVARELHRKGIY
PPINVLPSLSRLMNSGIGAGKTREDHKAVSDQMYAGYAEGRDLRGLVAIV
GKEALSERDTKFLEFADLFEDKFVRQGRNENRTIEDTLEIGWQILTHLPE
NQLGRIDNKYIQKYHPAHR
3D structure
PDB3dsr Structure of the nucleotide-binding subunit B of the energy producer A1A0 ATP synthase in complex with adenosine diphosphate
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H156 I185 T186 R349
Catalytic site (residue number reindexed from 1) H135 I164 T165 R311
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
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 F149 M305 P315 L317 S318 I321 Q325 F128 M273 P277 L279 S280 I283 Q287
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0033178 proton-transporting two-sector ATPase complex, catalytic domain

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Cellular Component
External links
PDB RCSB:3dsr, PDBe:3dsr, PDBj:3dsr
PDBsum3dsr
PubMed19020348
UniProtQ60187|VATB_METMA V-type ATP synthase beta chain (Gene Name=atpB)

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