|
eF-site ID
|
1bpl-AB |
PDB Code
|
1bpl |
Chain
|
A, B |
|
click to enlarge
|
|
Title
|
GLYCOSYLTRANSFERASE |
Classification
|
GLYCOSYLTRANSFERASE |
Compound
|
ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE |
Source
|
ORGANISM_SCIENTIFIC: Bacillus licheniformis; |
|
Sequence
|
A: |
LNGTLMQYFEWYMPNDGQHWKRLQNDSAYLAEHGITAVWI
PPAYKGTSQADVGYGAYDLYDLGEFHQKGTVRTKYGTKGE
LQSAIKSLHSRDINVYGDVVINHKGGADATEDVTAVEVDP
ADRNRVISGEHLIKAWTHFHFPGRGSTYSDFKWHWYHFDG
TDWDESRKLNRIYKFQGKA
|
B: |
YDYLMYADIDYDHPDVAAEIKRWGTWYANELQLDGFRLDA
VKHIKFSFLRDWVNHVREKTGKEMFTVAEYWQNDLGALEN
YLNKTNFNHSVFDVPLHYQFHAASTQGGGYDMRKLLNSTV
VSKHPLKAVTFVDNHDTQPGQSLESTVQTWFKPLAYAFIL
TRESGYPQVFYGDMYGTKGDSQREIPALKHKIEPILKARK
QYAYGAQHDYFDHHDIVGWTREGDSSVANSGLAALITDGP
GGAKRMYVGRQNAGETWHDITGNRSEPVVINSEGWGEFHV
NGGSVSIYVQ
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
B |
residue |
231 |
type |
|
sequence |
D
|
description |
ACTIVE SITE CATALYTIC RESIDUES
|
source |
: ACT
|
|
2)
|
chain |
B |
residue |
261 |
type |
|
sequence |
E
|
description |
ACTIVE SITE CATALYTIC RESIDUES
|
source |
: ACT
|
|
3)
|
chain |
B |
residue |
328 |
type |
|
sequence |
D
|
description |
ACTIVE SITE CATALYTIC RESIDUES
|
source |
: ACT
|
|
4)
|
chain |
B |
residue |
328 |
type |
SITE |
sequence |
D
|
description |
Transition state stabilizer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
5)
|
chain |
B |
residue |
194 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
6)
|
chain |
B |
residue |
200 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
7)
|
chain |
B |
residue |
204 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
8)
|
chain |
B |
residue |
300 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
9)
|
chain |
B |
residue |
302 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
10)
|
chain |
B |
residue |
406 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
11)
|
chain |
B |
residue |
407 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
12)
|
chain |
B |
residue |
430 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
13)
|
chain |
B |
residue |
202 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
14)
|
chain |
B |
residue |
235 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
15)
|
chain |
A |
residue |
181 |
type |
ACT_SITE |
sequence |
A
|
description |
Nucleophile
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
B |
residue |
231 |
type |
ACT_SITE |
sequence |
D
|
description |
Nucleophile
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
B |
residue |
261 |
type |
ACT_SITE |
sequence |
E
|
description |
Proton donor
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|