|
|
eF-site ID
|
4rva-A |
|
PDB Code
|
4rva |
|
Chain
|
A |
|
click to enlarge
|
|
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Title
|
A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for deacylation |
|
Classification
|
HYDROLASE |
|
Compound
|
Beta-lactamase TEM |
|
Source
|
Escherichia coli (BLAT_ECOLX) |
|
|
Sequence
|
A: |
HPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEER
FPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEY
SPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGP
KELTAFLHNMGDHVTRLDRYYGELNEAIPNDERDTTMPAA
MATTLRKLLTGELLTPASRQQLIDWMEADKVAGPLLRSAL
PAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTG
SQATMDERNRQIAEIGASLIKHW
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
69 |
| type |
|
| sequence |
M
|
| description |
BINDING SITE FOR RESIDUE BCT A 301
|
| source |
: AC1
|
|
|
2)
|
chain |
A |
| residue |
70 |
| type |
|
| sequence |
S
|
| description |
BINDING SITE FOR RESIDUE BCT A 301
|
| source |
: AC1
|
|
|
3)
|
chain |
A |
| residue |
130 |
| type |
|
| sequence |
S
|
| description |
BINDING SITE FOR RESIDUE BCT A 301
|
| source |
: AC1
|
|
|
4)
|
chain |
A |
| residue |
236 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE BCT A 301
|
| source |
: AC1
|
|
|
5)
|
chain |
A |
| residue |
237 |
| type |
|
| sequence |
A
|
| description |
BINDING SITE FOR RESIDUE BCT A 301
|
| source |
: AC1
|
|
|
6)
|
chain |
A |
| residue |
70 |
| type |
catalytic |
| sequence |
S
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
A |
| residue |
73 |
| type |
catalytic |
| sequence |
K
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
8)
|
chain |
A |
| residue |
130 |
| type |
catalytic |
| sequence |
S
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
9)
|
chain |
A |
| residue |
166 |
| type |
catalytic |
| sequence |
Y
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
10)
|
chain |
A |
| residue |
234 |
| type |
catalytic |
| sequence |
K
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
11)
|
chain |
A |
| residue |
237 |
| type |
catalytic |
| sequence |
A
|
| description |
2
|
| source |
MCSA : MCSA1
|
|
|
12)
|
chain |
A |
| residue |
70 |
| type |
ACT_SITE |
| sequence |
S
|
| description |
Acyl-ester intermediate
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
13)
|
chain |
A |
| residue |
168 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Proton acceptor
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
14)
|
chain |
A |
| residue |
66-81 |
| type |
prosite |
| sequence |
FPMMSTFKVLLCGAVL
|
| description |
BETA_LACTAMASE_A Beta-lactamase class-A active site. FpMMSTfKvllCGAVL
|
| source |
prosite : PS00146
|
|
|
15)
|
chain |
A |
| residue |
234 |
| type |
BINDING |
| sequence |
K
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
|