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6IW6

Crystal structure of the Lin28-interacting module of human TUT4

Functional Information from GO Data
ChainGOidnamespacecontents
A0016779molecular_functionnucleotidyltransferase activity
B0016779molecular_functionnucleotidyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS306
ACYS309
AHIS322
AHIS328

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS507
AHIS726
AHIS728
AHIS730

site_idAC3
Number of Residues7
Detailsbinding site for residue FLC A 1003
ChainResidue
AGLN512
AARG669
AARG670
AHIS729
AHIS731
AEDO1004
ASER511

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 1004
ChainResidue
ACYS507
ATYR508
AASP510
AARG670
AGLN690
AHIS728
AFLC1003

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 1005
ChainResidue
AALA476
ATHR480

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 1006
ChainResidue
APRO347
ATYR704

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BCYS306
BCYS309
BHIS322
BHIS328

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 1002
ChainResidue
BCYS507
BHIS726
BHIS728
BHIS730

site_idAC9
Number of Residues7
Detailsbinding site for residue FLC B 1003
ChainResidue
BSER511
BGLN512
BARG669
BARG670
BHIS729
BHIS731
BEDO1004

site_idAD1
Number of Residues8
Detailsbinding site for residue EDO B 1004
ChainResidue
BCYS507
BTYR508
BASP510
BARG670
BSER689
BGLN690
BHIS728
BFLC1003

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO B 1005
ChainResidue
BLYS552
BLEU659

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 1006
ChainResidue
BTRP503
BLYS505
BPHE722

site_idAD4
Number of Residues1
Detailsbinding site for residue EDO B 1007
ChainResidue
BTYR704

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO B 1008
ChainResidue
BPRO539
BTRP545
BPRO618
BALA620
BLEU621

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues23
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Ckl..ClihIeniqgahkHikekrH
ChainResidueDetails
ACYS306-HIS328

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsZN_FING: Matrin-type => ECO:0000255|PROSITE-ProRule:PRU00130
ChainResidueDetails
ATYR304-GLU334
BTYR304-GLU334

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31036859
ChainResidueDetails
ACYS306
ACYS309
AHIS322
AHIS328
BCYS306
BCYS309
BHIS322
BHIS328

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PDB entries from 2024-07-31

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