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5K97

Flap endonuclease 1 (FEN1) D233N with cleaved product fragment and Sm3+

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SM A 401
ChainResidue
AGLY2
AGLU160
AASP181
ASM403
ASM404
AHOH689
EDT7

site_idAC2
Number of Residues6
Detailsbinding site for residue SM A 402
ChainResidue
AGLU160
ASM404
AHOH525
EHOH113
AASP86
AGLU158

site_idAC3
Number of Residues5
Detailsbinding site for residue SM A 403
ChainResidue
AGLU160
AASP179
AASP181
ASM401
EDT7

site_idAC4
Number of Residues8
Detailsbinding site for residue SM A 404
ChainResidue
AGLU158
AGLU160
ASM401
ASM402
AHOH525
EDT7
EHOH103
EHOH113

site_idAC5
Number of Residues6
Detailsbinding site for residue K A 405
ChainResidue
ASER237
AILE238
AILE241
AHOH640
DDT5
DHOH131

site_idAC6
Number of Residues7
Detailsbinding site for residue SM A 406
ChainResidue
AGLU57
AGLU285
AGLU313
AGLN342
AHOH537
AHOH588
AHOH598

site_idAC7
Number of Residues7
Detailsbinding site for residue SM A 407
ChainResidue
AGLU57
AGLU59
AGLU313
AGLN342
AHOH589
AHOH639
AHOH668

site_idAC8
Number of Residues4
Detailsbinding site for residue SM A 408
ChainResidue
AGLY49
AASP51
AHOH724
AHOH803

site_idAC9
Number of Residues4
Detailsbinding site for residue SM A 409
ChainResidue
AGLU102
AHOH545
AHOH891
AHOH901

site_idAD1
Number of Residues6
Detailsbinding site for residue EDO A 410
ChainResidue
AGLY2
AILE3
AASP179
AMET180
AHOH596
EDG8

Functional Information from PROSITE/UniProt
site_idPS00841
Number of Residues15
DetailsXPG_1 XPG protein signature 1. IKPvYVFDGkpPqLK
ChainResidueDetails
AILE79-LYS93

site_idPS00842
Number of Residues15
DetailsXPG_2 XPG protein signature 2. GIPYLdAPsEAEASC
ChainResidueDetails
AGLY149-CYS163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1
ChainResidueDetails
AASP34

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AARG47
AARG70
AGLY231

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7
ChainResidueDetails
AASP86
AGLU158

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD
ChainResidueDetails
AGLU160
AASP181

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD
ChainResidueDetails
AASP179

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:5ZOD
ChainResidueDetails
AASN233

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856
ChainResidueDetails
AARG19
AARG100
AARG104
AARG192

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS80

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK2 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856
ChainResidueDetails
ASER187

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER197

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER255
ASER293
ASER335

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR336

217705

PDB entries from 2024-03-27

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