Structure of PDB 7r94 Chain E

Receptor sequence
>7r94E (length=370) Species: 9031 (Gallus gallus) [Search protein sequence]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWITKQEYDEAGPSIVHRKC
3D structure
PDB7r94 Structural mechanism for bidirectional actin cross-linking by T-plastin.
ChainE
Resolution2.6 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.4.-
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 E G13 G15 L16 K18 G156 D157 K213 E214 G302 Y306 G9 G11 L12 K14 G152 D153 K209 E210 G298 Y302
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Biological Process
GO:0030240 skeletal muscle thin filament assembly
GO:0048741 skeletal muscle fiber development
Cellular Component
GO:0001725 stress fiber
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005865 striated muscle thin filament
GO:0005884 actin filament

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7r94, PDBe:7r94, PDBj:7r94
PDBsum7r94
PubMed36067297
UniProtP68139|ACTS_CHICK Actin, alpha skeletal muscle (Gene Name=ACTA1)

[Back to BioLiP]