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6CA4

Crystal structure of humanized D. rerio TDP2 by 14 mutations

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
B0003824molecular_functioncatalytic activity
C0003824molecular_functioncatalytic activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 401
ChainResidue
AASP131
AGLU161
AHOH513
AHOH526
AHOH553
AHOH652

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO A 402
ChainResidue
BTHR210
BTHR211
ALYS122
AASP341
ATHR366

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 403
ChainResidue
AGLU202
AGLU204
AILE219
AGLN221
ATYR230
AHOH502

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU300
AHIS301
AARG303
ATYR304
AMET348
AHOH532

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO A 405
ChainResidue
APHE208
APRO209
ATHR210
ATHR211
AGLU245
ALYS248

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
ALYS195
AALA332
ALYS333
AALA335
AHOH605

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO A 407
ChainResidue
AGLU181
ASER203
AHOH520

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 408
ChainResidue
AARG173
AALA174
AEDO409
AHOH519

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 409
ChainResidue
ATHR153
AEDO408
AHOH519
AHOH606

site_idAD1
Number of Residues5
Detailsbinding site for residue MG B 401
ChainResidue
BASP131
BGLU161
BHOH505
BHOH525
BHOH575

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO B 402
ChainResidue
BPHE208
BPRO209
BTHR210
BGLU245
BGLN249
BVAL252

site_idAD3
Number of Residues6
Detailsbinding site for residue EDO B 403
ChainResidue
BLEU274
BLEU322
BARG323
BARG326
BMLI404
BHOH538

site_idAD4
Number of Residues9
Detailsbinding site for residue MLI B 404
ChainResidue
BASP276
BALA277
BARG323
BARG326
BEDO403
BHOH512
BHOH538
BHOH548
BHOH559

site_idAD5
Number of Residues6
Detailsbinding site for residue MG C 401
ChainResidue
CASP131
CGLU161
CHOH510
CHOH524
CHOH592
CHOH629

site_idAD6
Number of Residues7
Detailsbinding site for residue EDO C 402
ChainResidue
AGLY283
AHOH501
CGLU181
CSER203
CGLU204
CLEU218
CHOH573

site_idAD7
Number of Residues4
Detailsbinding site for residue EDO C 403
ChainResidue
CARG330
CSER331
CLYS333
CHOH522

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O95551
ChainResidueDetails
AASP271
BASP271
CASP271

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9JJX7
ChainResidueDetails
AASP131
BASP131
CASP131

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23104058, ECO:0007744|PDB:4FPV
ChainResidueDetails
AGLU161
BGLU161
CGLU161

site_idSWS_FT_FI4
Number of Residues9
DetailsSITE: Interaction with 5' end of substrate DNA => ECO:0000250|UniProtKB:Q9JJX7
ChainResidueDetails
ATYR187
ATRP306
APHE324
BTYR187
BTRP306
BPHE324
CTYR187
CTRP306
CPHE324

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Interaction with 5' end of substrate DNA => ECO:0000269|PubMed:23104058
ChainResidueDetails
AHIS360
BHIS360
CHIS360

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PDB entries from 2024-07-24

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