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6QPL

Crystal structure of Spindlin1 in complex with the inhibitor MS31

Functional Information from GO Data
ChainGOidnamespacecontents
B0007276biological_processgamete generation
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MPD B 301
ChainResidue
BGLY153
BMET154
BGLU171
BVAL242
BVAL255
BHOH424
BHOH432

site_idAC2
Number of Residues4
Detailsbinding site for residue MPD B 302
ChainResidue
BTYR98
BHOH486
BTRP62
BTRP72

site_idAC3
Number of Residues4
Detailsbinding site for residue DMS B 303
ChainResidue
BPRO81
BTYR185
BLYS186
BGLY188

site_idAC4
Number of Residues1
Detailsbinding site for residue DMS B 304
ChainResidue
BJC5305

site_idAC5
Number of Residues11
Detailsbinding site for residue JC5 B 305
ChainResidue
BASP95
BHIS139
BPHE141
BTRP151
BTYR170
BTYR177
BTYR179
BASP184
BDMS304
BHOH425
BHOH487

site_idAC6
Number of Residues2
Detailsbinding site for residue GLY B 306
ChainResidue
BARG191
BGLN269

site_idAC7
Number of Residues5
Detailsbinding site for residue PO4 B 307
ChainResidue
BGLU101
BARG107
BGLY146
BHOH415
BHOH422

site_idAC8
Number of Residues3
Detailsbinding site for residue GOL B 308
ChainResidue
BASP224
BGLY225
BSER226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Histone H3K4me3 and H3R8me2a binding
ChainResidueDetails
BASP173
BGLN180
BASP184

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by AURKA => ECO:0000269|PubMed:22258766
ChainResidueDetails
BSER109

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by AURKA => ECO:0000269|PubMed:22258766, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER124

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER199

218500

건을2024-04-17부터공개중

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