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4MZG

Crystal structure of human Spindlin1 bound to histone H3K4me3 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0030527molecular_functionstructural constituent of chromatin
B0007276biological_processgamete generation
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0030527molecular_functionstructural constituent of chromatin
D0007276biological_processgamete generation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD B 301
ChainResidue
AARG8
BTRP62
BTRP72
BTYR98
BHOH432
BHOH434

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B 302
ChainResidue
BASP257
BGLU171
BVAL242
BVAL255

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 303
ChainResidue
BHOH414
BHOH428
BHOH431
DHOH421
DHOH422
DHOH428

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 304
ChainResidue
BARG152
BLYS172

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD D 301
ChainResidue
DTRP62
DTRP72
DTYR98
DLEU100
DPHE251

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD D 302
ChainResidue
DMET154
DGLU171
DHOH502
DHOH526

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL D 303
ChainResidue
BARG152
DARG152
DLYS172

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 304
ChainResidue
DTRP165

Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsSITE: Histone H3K4me3 and H3R8me2a binding
ChainResidueDetails
BASP173
BGLN180
BASP184
DASP173
DGLN180
DASP184

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AURKA => ECO:0000269|PubMed:22258766
ChainResidueDetails
BSER109
DSER109

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AURKA => ECO:0000269|PubMed:22258766, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER124
DSER124
CM3L4
CLYS18

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER199
DSER199

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
ATHR6
CTHR6

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
AARG8
CARG8

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708
ChainResidueDetails
ALYS9
CLYS9

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
ChainResidueDetails
ASER10
CSER10

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803
ChainResidueDetails
ATHR11
CTHR11

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS14
CLYS14

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635
ChainResidueDetails
AARG17
CARG17

site_idSWS_FT_FI12
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
CLYS18

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PDB entries from 2024-07-17

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