Structure of PDB 5ksd Chain B

Receptor sequence
>5ksdB (length=833) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
VDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKF
LGFMWNPLSWVMEMAAIMAIALANGDGRPPDWQDFVGIICLLVINSTISF
IEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDI
IPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVV
IATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIV
MYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAIT
KRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLF
AAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTY
IDGSGNWHRVSKGAPEQILELAKASNDLSKKVLSIIDKYAERGLRSLAVA
RQVVPEKTKESPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMIT
GDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASIPVEELIEKADGF
AGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDA
ARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFM
LIALIWEFDFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFA
TGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDNNHELMGAVYLQV
SIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVYANWEFAK
IRGIGWGWAGVIWLYSIVTYFPLDVFKFAIRYI
3D structure
PDB5ksd Improved Model of Proton Pump Crystal Structure Obtained by Interactive Molecular Dynamics Flexible Fitting Expands the Mechanistic Model for Proton Translocation in P-Type ATPases.
ChainB
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D329 D588 D592
Catalytic site (residue number reindexed from 1) D318 D577 D581
Enzyme Commision number 7.1.2.1: P-type H(+)-exporting transporter.
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 ACP B T331 I374 F400 A425 L458 T511 T320 I363 F389 A414 L447 T500
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005215 transporter activity
GO:0005524 ATP binding
GO:0008553 P-type proton-exporting transporter activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0120029 proton export across plasma membrane
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ksd, PDBe:5ksd, PDBj:5ksd
PDBsum5ksd
PubMed28443028
UniProtP19456|PMA2_ARATH ATPase 2, plasma membrane-type (Gene Name=AHA2)

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