Structure of PDB 3tgw Chain B

Receptor sequence
>3tgwB (length=441) Species: 192952 (Methanosarcina mazei Go1) [Search protein sequence]
QIAGPLIFVEKTEPVGYNEIVNIKMGDGTVRRGQVLDSSADIVVVQVFEG
TGGVIFTGETLKLPASVDLLGRILSGSGEPRDGGPRIVPDQLLDINGAAM
NPYARLPPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPANEIALQIAR
QASVPGSESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADD
PAVERIVTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGAAPGR
RGYPGYMYTDLATLYERAGIVKGAKGSVTQIPILSMPGDDITHPIPDLSG
YITEGQIVVARELHRKGIYPPINVLPSLSRLMNSGIGAGKTREDHKAVSD
QMYAGYAEGRDLRGLVAIVGKEALSERDTKFLEFADLFEDKFVRQGRNEN
RTIEDTLEIGWQILTHLPENQLGRIDNKYIQKYHPAHRKAK
3D structure
PDB3tgw Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A1Ao ATP synthase
ChainB
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A156 I185 T186 R349
Catalytic site (residue number reindexed from 1) A141 I170 T171 R330
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 AES B K20 P23 V24 Y26 S47 K11 P14 V15 Y17 S38
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:3tgw, PDBe:3tgw, PDBj:3tgw
PDBsum3tgw
PubMed
UniProtQ60187|VATB_METMA V-type ATP synthase beta chain (Gene Name=atpB)

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