eF-site ID 6tka-.AAA
PDB Code 6tka
Chain AAA

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Title Crystal structure of human O-GlcNAc transferase bound to substrate 7 and a peptide from HCF-1 pro-repeat 2 (11-26)
Classification TRANSFERASE
Compound UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Source (6TKA)
Sequence AAA:  ACPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFA
AAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNM
GNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKD
SGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTD
YDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRK
AIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYV
SSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNF
RVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNG
YTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQ
ETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVI
DFIYDNRIVLNGIDLKAFLDSLPDVKIVKNMPVIPMNTIA
EAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEV
PRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWAN
ILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFS
PVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPM
VTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKL
GTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQM
WEHYAAGNKPDHMI
Description


Functional site

1) chain AAA
residue 624
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:21240259, ECO:0000305|PubMed:26678539
source Swiss-Prot : SWS_FT_FI1

2) chain AAA
residue 570
type MOD_RES
sequence M
description Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260
source Swiss-Prot : SWS_FT_FI3

3) chain AAA
residue 515
type CARBOHYD
sequence E
description O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473
source Swiss-Prot : SWS_FT_FI4

4) chain AAA
residue 965
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
source Swiss-Prot : SWS_FT_FI2

5) chain AAA
residue 968
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
source Swiss-Prot : SWS_FT_FI2

6) chain AAA
residue 1022
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
source Swiss-Prot : SWS_FT_FI2

7) chain AAA
residue 1027
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
source Swiss-Prot : SWS_FT_FI2


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