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5UND

Crystal Structure of CTCF(ZnF 4-10) With 28-mer DNA

Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 601
ChainResidue
ACYS353
ACYS356
AHIS369
AHIS373

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 602
ChainResidue
ACYS381
ACYS384
AHIS397
AHIS401

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 603
ChainResidue
ACYS412
AHIS425
AHIS430
ACYS409

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 604
ChainResidue
ACYS439
ACYS442
AHIS455
AHIS460

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 605
ChainResidue
ACYS469
ACYS472
AHIS485
AHIS489

site_idAC6
Number of Residues3
Detailsbinding site for residue ZN A 606
ChainResidue
ACYS500
AHIS513
AHIS517

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO D 101
ChainResidue
CDT11
DDG19

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO D 102
ChainResidue
CDG13
DDG15

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 601
ChainResidue
BCYS353
BCYS356
BHIS369
BHIS373

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 602
ChainResidue
BCYS381
BCYS384
BHIS397
BHIS401

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 603
ChainResidue
BCYS409
BCYS412
BHIS425
BHIS430

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN B 604
ChainResidue
BCYS439
BCYS442
BHIS455
BHIS460

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN B 605
ChainResidue
BCYS469
BCYS472
BHIS485
BHIS489

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO B 606
ChainResidue
BCYS412
BHIS425
BLYS429

site_idAD6
Number of Residues3
Detailsbinding site for residue GOL B 607
ChainResidue
BHIS441
BHIS460
BGLU478

site_idAD7
Number of Residues2
Detailsbinding site for residue EDO E 101
ChainResidue
EDT11
FDG19

site_idAD8
Number of Residues1
Detailsbinding site for residue EDO F 101
ChainResidue
FDG15

site_idAD9
Number of Residues1
Detailsbinding site for residue EDO F 102
ChainResidue
FDG14

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues22
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cyi..CharFtqsgtmkmHilqk.H
ChainResidueDetails
ACYS409-HIS430
ACYS439-HIS460
ACYS469-HIS489
ACYS497-HIS517
ACYS525-HIS546

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsZN_FING: C2H2-type 4 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
APHE351-HIS373
BPHE351-HIS373

site_idSWS_FT_FI2
Number of Residues44
DetailsZN_FING: C2H2-type 5 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
APHE379-HIS401
BPHE379-HIS401

site_idSWS_FT_FI3
Number of Residues46
DetailsZN_FING: C2H2-type 6 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
ATYR407-HIS430
BTYR407-HIS430

site_idSWS_FT_FI4
Number of Residues46
DetailsZN_FING: C2H2-type 7 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
APHE437-HIS460
BPHE437-HIS460

site_idSWS_FT_FI5
Number of Residues44
DetailsZN_FING: C2H2-type 8 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
ALYS467-HIS489
BLYS467-HIS489

site_idSWS_FT_FI6
Number of Residues44
DetailsZN_FING: C2H2-type 9 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
APHE495-HIS517
BPHE495-HIS517

site_idSWS_FT_FI7
Number of Residues46
DetailsZN_FING: C2H2-type 10 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
ATYR523-HIS546
BTYR523-HIS546

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR374
BTHR374

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER402
BSER402

219869

PDB entries from 2024-05-15

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