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4KIT

Crystal structure of human Brr2 in complex with the Prp8 Jab1/MPN domain

Functional Information from GO Data
ChainGOidnamespacecontents
B0003676molecular_functionnucleic acid binding
B0005524molecular_functionATP binding
C0000398biological_processmRNA splicing, via spliceosome
C0005681cellular_componentspliceosomal complex
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ADP B 2201
ChainResidue
BTHR480
BGLN485
BGLY508
BLYS509
BTHR510
BASP615
BGLU616
BASN820

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP B 2202
ChainResidue
BPHE1327
BGLN1332
BGLY1353
BSER1354
BGLY1355
BLYS1356
BTHR1357
BGLU1455
BPRO1694
BMG2203
BPHE1325

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2203
ChainResidue
BTHR1357
BASP1454
BADP2202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues183
DetailsDomain: {"description":"Helicase ATP-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues237
DetailsDomain: {"description":"Helicase C-terminal 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues305
DetailsDomain: {"description":"SEC63 1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues175
DetailsDomain: {"description":"Helicase ATP-binding 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues208
DetailsDomain: {"description":"Helicase C-terminal 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues312
DetailsDomain: {"description":"SEC63 2"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsMotif: {"description":"DEIH box"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsMotif: {"description":"DEVH box"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23045696","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F93","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"F1LNJ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6P4T2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues131
DetailsDomain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues34
DetailsRegion: {"description":"Required for interaction with EFTUD2 and SNRNP200","evidences":[{"source":"PubMed","id":"17317632","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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