Structure of PDB 3tiv Chain B

Receptor sequence
>3tivB (length=430) Species: 192952 (Methanosarcina mazei Go1) [Search protein sequence]
IAGPLIFVEKTEPVGYNEIVNIKMGDGTVRRGQVLDSSADIVVVQVFEGV
IFTGETLKLPASVDLLGRILSGSGEPRDGGPRIVPDQLLDINGAAMNPYA
RLPPKDFIQTGISTIDGTNTLVRGQKLPIFSASGLPHAEIALQIARQASV
PGSESAFAVVFAAMGITNEEAQYFMSDFEKTGALERAVVFLNLADDPAVE
RIVTPRMALTAAEYLAYEHGMHVLVILTDITNYAEALRQMGYPGYMYTDL
ATLYERAGIVKGAKGSVTQIPILSMPGDDITHPIPDLSGYITEGQIVVAR
ELHRKGIYPPINVLPSLSRLMNSGIGAGKTREDHKAVSDQMYAGYAEGRD
LRGLVAIVGKEALSERDTKFLEFADLFEDKFVRQGRNENRTIEDTLEIGW
QILTHLPENQLGRIDNKYIQKYHPAHRKAK
3D structure
PDB3tiv 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) H156 I185 T186 R349
Catalytic site (residue number reindexed from 1) H137 I166 T167 R319
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 K10 P13 V14 Y16 S37
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:3tiv, PDBe:3tiv, PDBj:3tiv
PDBsum3tiv
PubMed
UniProtQ60187|VATB_METMA V-type ATP synthase beta chain (Gene Name=atpB)

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