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8Y6K

Cryo-EM structure of full-length MICAL1 in the autoinhibited state

Functional Information from PROSITE/UniProt
site_idPS00478
Number of Residues35
DetailsLIM_DOMAIN_1 LIM zinc-binding domain signature. CalCgehlyvlerlcvnghf.....FHrsCfrChtCeatL
ChainResidueDetails
ACYS697-LEU731

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8VDP3
ChainResidueDetails
ACYS95
AGLU114
AARG121
APHE181
ATYR293
AASP393

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0007744|PDB:2CO8
ChainResidueDetails
ACYS697
ACYS700
AHIS718
ACYS721
ACYS724
ACYS727
ACYS747
AHIS750

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for interaction with ARHGAP26 AND ARHGAP10 => ECO:0000269|PubMed:32344433
ChainResidueDetails
ALYS832

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:D3ZBP4
ChainResidueDetails
ATHR475

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER617

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER872

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER875
ASER876

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1057

225946

PDB entries from 2024-10-09

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