|
|
eF-site ID
|
1bvv-A |
|
PDB Code
|
1bvv |
|
Chain
|
A |
|
click to enlarge
|
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Title
|
SUGAR RING DISTORTION IN THE GLYCOSYL-ENZYME INTERMEDIATE OF A FAMILY G/11 XYLANASE |
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Classification
|
HYDROLASE |
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Compound
|
ENDO-1,4-BETA-XYLANASE |
|
Source
|
Bacillus circulans (XYNA_BACCI) |
|
|
Sequence
|
A: |
ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGK
GWTTGSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYY
VVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDG
DRTTFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNL
GSNWAYQVMATEGYQSSGSSNVTVW
|
|
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Description
|
(1) |
ENDO-1,4-BETA-XYLANASE, 1,2-DEOXY-2-FLUORO-XYLOPYRANOSE
|
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Functional site
|
|
|
1)
|
chain |
A |
| residue |
78 |
| type |
|
| sequence |
E
|
| description |
THE NUCLEOPHILE TO WHICH THE INHIBITOR IS BOUND IS GLU 78.
|
| source |
: NUC
|
|
|
2)
|
chain |
A |
| residue |
172 |
| type |
|
| sequence |
E
|
| description |
THE ACID BASE CATALYST IS RESIDUE GLU 172.
|
| source |
: ABC
|
|
|
3)
|
chain |
A |
| residue |
35 |
| type |
catalytic |
| sequence |
N
|
| description |
432
|
| source |
MCSA : MCSA1
|
|
|
4)
|
chain |
A |
| residue |
69 |
| type |
catalytic |
| sequence |
Y
|
| description |
432
|
| source |
MCSA : MCSA1
|
|
|
5)
|
chain |
A |
| residue |
78 |
| type |
catalytic |
| sequence |
E
|
| description |
432
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
A |
| residue |
80 |
| type |
catalytic |
| sequence |
Y
|
| description |
432
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
A |
| residue |
172 |
| type |
catalytic |
| sequence |
E
|
| description |
432
|
| source |
MCSA : MCSA1
|
|
|
8)
|
chain |
A |
| residue |
75-85 |
| type |
prosite |
| sequence |
PLIEYYVVDSW
|
| description |
GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYVVDsW
|
| source |
prosite : PS00776
|
|
|
9)
|
chain |
A |
| residue |
169-180 |
| type |
prosite |
| sequence |
MATEGYQSSGSS
|
| description |
GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
|
| source |
prosite : PS00777
|
|
|
10)
|
chain |
A |
| residue |
78 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
11)
|
chain |
A |
| residue |
172 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|