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5CQH

Crystal Structure of the Cancer Genomic DNA Mutator APOBEC3B

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS253
ACYS284
ACYS289
AEDO405

site_idAC2
Number of Residues13
Detailsbinding site for residue DC A 402
ChainResidue
AARG372
AHOH504
AHOH549
AHOH554
AHOH559
AHOH598
AHOH616
AHOH620
AARG252
AASP260
AASP314
ATYR319
ALYS320

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 403
ChainResidue
AILE335
ASER370
AARG374

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 404
ChainResidue
APRO206
AARG252
ATRP287
AGLU292
AHOH510
AHOH580

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 405
ChainResidue
ATHR214
AHIS253
AGLU255
ASER282
ACYS284
ACYS289
AZN401

site_idAC6
Number of Residues6
Detailsbinding site for residue EDO A 406
ChainResidue
ACYS239
ATHR337
ATYR338
AASP339
AHOH560
AHOH562

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 407
ChainResidue
AASP339
AGLU340
ATYR343
AHOH516
AHOH622
AHOH640

Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues41
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAElrFLdlvpslqldpaqiyrvtwfisws..........PCfswg....CageV
ChainResidueDetails
AHIS253-VAL293

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
APRO263

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALEU261
AGLU292
ALEU297

224004

PDB entries from 2024-08-21

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