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4OUC

Structure of human haspin in complex with histone H3 substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 801
ChainResidue
AGLU554
APHE556
ASER684
AHOH1107
AHOH1108

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 802
ChainResidue
AHOH1133
AILE610
AMET615
ALEU657
AHOH1125

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 803
ChainResidue
ATHR553
AGLY555
AGLN631
ASER635
AGLN682
AHOH1045
AHOH1143

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 804
ChainResidue
ALEU520
APHE593

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 805
ChainResidue
AGLU728
ATYR739
AHOH1016
AHOH1167

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 806
ChainResidue
APHE475
AGLY567
ASER568
AHOH923
AHOH931

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 807
ChainResidue
ALYS761
ACYS762
ALYS771
AHOH1177
AHOH1293

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 5ID A 808
ChainResidue
AILE490
AGLY491
AGLU492
AVAL498
AALA509
APHE605
AGLU606
APHE607
AGLY608
AGLY609
AASP611
AGLY653
ALEU656
AILE686
AIOD809
AHOH912
AHOH951
AHOH1130

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD A 809
ChainResidue
ALYS511
APHE605
AASP687
A5ID808

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGVFGEVFqTiadhtp............VAIK
ChainResidueDetails
AILE490-LYS511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
BARG2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
ChainResidueDetails
BTHR3
ALYS511

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS4
AASP649

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
BGLN5

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
BTHR6

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
BARG8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS9

site_idSWS_FT_FI8
Number of Residues1
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
BSER10

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803
ChainResidueDetails
BTHR11

218853

PDB entries from 2024-04-24

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