|
eF-site ID
|
2fyd-ABCD |
PDB Code
|
2fyd |
Chain
|
A, B, C, D |
|
click to enlarge
|
|
Title
|
catalytic domain of bovine beta 1, 4-galactosyltransferase in complex with alpha-lactalbumin, glucose, Mn, and UDP-N-acetylgalactosamine |
Classification
|
TRANSFERASE |
Compound
|
Alpha-lactalbumin |
Source
|
(AAM54035) |
|
Sequence
|
A: |
TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA
VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL
LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC
EKP
|
B: |
LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR
YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ
LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF
SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF
GGVSALSKQQFLSINGFPNNYCGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETM
LSDGLNSLTYMVLEVQRYPLYTKITVDIGTCS
|
C: |
TELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQA
VVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKL
LDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRC
EKP
|
D: |
LTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGR
YTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQ
LDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVF
SDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYF
GGVSALSKQQFLSINGFPNNYCGWGGEDDDIYNRLAFRGM
SVSRPNAVIGKTRMIRHSRDKKNEPNPQRFDRIAHTKETM
LSDGLNSLTYMVLEVQRYPLYTKITVDIGTCS
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
B |
residue |
252 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
B |
residue |
254 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
B |
residue |
314 |
type |
catalytic |
sequence |
W
|
description |
570
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
B |
residue |
317 |
type |
catalytic |
sequence |
E
|
description |
570
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
B |
residue |
318 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
B |
residue |
344 |
type |
catalytic |
sequence |
M
|
description |
570
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
B |
residue |
347 |
type |
catalytic |
sequence |
H
|
description |
570
|
source |
MCSA : MCSA1
|
|
8)
|
chain |
B |
residue |
349 |
type |
catalytic |
sequence |
R
|
description |
570
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
D |
residue |
252 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA2
|
|
10)
|
chain |
D |
residue |
254 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA2
|
|
11)
|
chain |
D |
residue |
314 |
type |
catalytic |
sequence |
W
|
description |
570
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
D |
residue |
317 |
type |
catalytic |
sequence |
E
|
description |
570
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
D |
residue |
318 |
type |
catalytic |
sequence |
D
|
description |
570
|
source |
MCSA : MCSA2
|
|
14)
|
chain |
D |
residue |
344 |
type |
catalytic |
sequence |
M
|
description |
570
|
source |
MCSA : MCSA2
|
|
15)
|
chain |
D |
residue |
347 |
type |
catalytic |
sequence |
H
|
description |
570
|
source |
MCSA : MCSA2
|
|
16)
|
chain |
D |
residue |
349 |
type |
catalytic |
sequence |
R
|
description |
570
|
source |
MCSA : MCSA2
|
|
17)
|
chain |
A |
residue |
73-91 |
type |
prosite |
sequence |
CGISCDKLLDDELDDDIAC
|
description |
GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgisCdkLlddELdddiaC
|
source |
prosite : PS00128
|
|
18)
|
chain |
B |
residue |
187 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
D |
residue |
226 |
type |
BINDING |
sequence |
F
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
20)
|
chain |
D |
residue |
253 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
21)
|
chain |
D |
residue |
254 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
22)
|
chain |
D |
residue |
314 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
D |
residue |
316 |
type |
BINDING |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
24)
|
chain |
D |
residue |
347 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
25)
|
chain |
D |
residue |
359 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
26)
|
chain |
B |
residue |
226 |
type |
BINDING |
sequence |
F
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
27)
|
chain |
B |
residue |
253 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
28)
|
chain |
B |
residue |
254 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
29)
|
chain |
B |
residue |
314 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
30)
|
chain |
B |
residue |
316 |
type |
BINDING |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
B |
residue |
347 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
B |
residue |
359 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
33)
|
chain |
D |
residue |
187 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
34)
|
chain |
A |
residue |
45 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
35)
|
chain |
C |
residue |
45 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|