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5URJ

Crystal structure of human BRR2 in complex with T-3905516

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 2201
ChainResidue
ALYS1199
AGLY1460
AHIS1727
ATYR1770
A8LS2202

site_idAC2
Number of Residues17
Detailsbinding site for residue 8LS A 2202
ChainResidue
AVAL1256
APRO1257
AASP1678
ATYR1679
APRO1680
AILE1681
ASER1709
ALYS1710
AASP1712
APHE1713
ALYS1716
APRO1723
AGOL2201
ATHR1197
AHIS1235
APHE1254
APHE1255

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541, ECO:0000269|PubMed:23045696, ECO:0007744|PDB:4F93
ChainResidueDetails
AALA503
AALA1350

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:F1LNJ2
ChainResidueDetails
ATYR709

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS971

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR1428

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P4T2
ChainResidueDetails
ATHR1765

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2002

221051

PDB entries from 2024-06-12

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