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5B64

A novel binding mode of MAGUK GK domain revealed by DLG GK domain in complex with KIF13B MBS domain

Functional Information from GO Data
ChainGOidnamespacecontents
B0003777molecular_functionmicrotubule motor activity
B0007018biological_processmicrotubule-based movement
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue SO4 A 801
ChainResidue
AARG637
AARG637

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 802
ChainResidue
AHIS596
AGLU600
ASER631
AASN633
AARG637
AHOH901

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 803
ChainResidue
AARG571
AHIS607
AARG568

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 804
ChainResidue
AVAL583
ASER584
ASER585

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 805
ChainResidue
AGLY541
APRO542
ATHR543
ALYS544
AASP545
AHOH904

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 806
ChainResidue
AHIS565
AASP592
ALYS597

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 807
ChainResidue
AARG586
AGLU587
AGLU590
AGLU686
APHE688
ASER689

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 B 801
ChainResidue
BASP776
BPRO778
BARG781

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRpkReyEidGrdYhFV
ChainResidueDetails
ATHR566-VAL583

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q62108
ChainResidueDetails
ATYR580

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q62108
ChainResidueDetails
ASER606

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER654

221051

PDB entries from 2024-06-12

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