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3EL2

Crystal Structure of Monomeric Actin Bound to Ca-ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000281biological_processmitotic cytokinesis
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0006338biological_processchromatin remodeling
A0007291biological_processsperm individualization
A0016787molecular_functionhydrolase activity
A0030723biological_processovarian fusome organization
A0031011cellular_componentIno80 complex
A0032507biological_processmaintenance of protein location in cell
A0035060cellular_componentbrahma complex
A0035148biological_processtube formation
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY302
ATHR303
AMET305
ALYS336
ACA901
AHOH967
ASER14
AHOH988
AHOH1019
AHOH1078
AHOH1093
AGLY15
AMET16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 901
ChainResidue
AATP800
AHOH929
AHOH1015
AHOH1019
AHOH1092
AHOH1093

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 902
ChainResidue
AGLN225
AGLN263
ASER265
AHOH1025
AHOH1056

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylaspartate => ECO:0000250
ChainResidueDetails
AASP2

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Methionine sulfoxide => ECO:0000269|PubMed:22116028
ChainResidueDetails
AMET44
AMET47

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Tele-methylhistidine => ECO:0000250|UniProtKB:P02572
ChainResidueDetails
AHIS73

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PDB entries from 2024-07-17

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