Structure of PDB 4pjl Chain A

Receptor sequence
>4pjlA (length=760) Species: 9823 (Sus scrofa) [Search protein sequence]
KPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEED
SKKDVEDNCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIP
KIYSSETIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKLSQSIIVSGESG
AGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSS
RFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAG
ASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYLKAG
SLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEE
AGSTSGGCNLKNKSTQALEYCAELLGLDQDDLRVSLTTRVMVIKVPLKVE
QANNARDALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIEGFEYFE
HNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDC
IDLIEARLVGILDILDEENRLPQPSDQHFTSAVHQKHKDHFRLSIPRKSK
LAIHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRD
KFIRELFELSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHH
FEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPDKLARL
DPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAE
LVKRVNHWLI
3D structure
PDB4pjl How actin initiates the motor activity of Myosin.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S153 G154 T158 N200 S203 S204 G459 E461
Catalytic site (residue number reindexed from 1) S149 G150 T154 N196 S199 S200 G445 E447
Enzyme Commision number ?
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 MG A T158 S204 T154 S200
BS02 ADP A N98 P99 G154 G156 K157 T158 E159 N200 N94 P95 G150 G152 K153 T154 E155 N196
Gene Ontology
Molecular Function
GO:0003774 cytoskeletal motor activity
GO:0005524 ATP binding
GO:0051015 actin filament binding
Cellular Component
GO:0016459 myosin complex

View graph for
Molecular Function

View graph for
Cellular Component
External links
PDB RCSB:4pjl, PDBe:4pjl, PDBj:4pjl
PDBsum4pjl
PubMed25936506
UniProtF1RQI7

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