|
|
eF-site ID
|
1gpq-ABCD |
|
PDB Code
|
1gpq |
|
Chain
|
A, B, C, D |
|
click to enlarge
|
|
|
Title
|
Structure of ivy complexed with its target, HEWL |
|
Classification
|
HYDROLASE/INHIBITOR |
|
Compound
|
INHIBITOR OF VERTEBRATE LYSOZYME |
|
Source
|
ORGANISM_COMMON: CHICKEN; ORGANISM_SCIENTIFIC: GALLUS GALLUS; |
|
|
Sequence
|
A: |
DDLTISSLAKGETTKAAFNQMVQGHKLPAWVMKGGTYTPA
QTVTLGDETYQVMSACKPHDCGSQRIAVMWSEKSNQMTGL
FSTIDEKTSQEKLTWLNVNDALSIDGKTVLFAALTGSLEN
HPDGFNF
|
| B: |
DDLTISSLAKGETTKAAFNQMVQGHKLPAWVMKGGTYTPA
QTVTLGDETYQVMSACKPHDCGSQRIAVMWSEKSNQMTGL
FSTIDEKTSQEKLTWLNVNDALSIDGKTVLFAALTGSLEN
HPDGFNFR
|
| C: |
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNT
QATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV
QAWIRGC
|
| D: |
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNT
QATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPC
SALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV
QAWIRGCR
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
C |
| residue |
35 |
| type |
catalytic |
| sequence |
E
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
2)
|
chain |
C |
| residue |
46 |
| type |
catalytic |
| sequence |
N
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
3)
|
chain |
C |
| residue |
48 |
| type |
catalytic |
| sequence |
D
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
4)
|
chain |
C |
| residue |
50 |
| type |
catalytic |
| sequence |
S
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
5)
|
chain |
C |
| residue |
52 |
| type |
catalytic |
| sequence |
D
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
C |
| residue |
59 |
| type |
catalytic |
| sequence |
N
|
| description |
203
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
D |
| residue |
35 |
| type |
catalytic |
| sequence |
E
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
8)
|
chain |
D |
| residue |
46 |
| type |
catalytic |
| sequence |
N
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
9)
|
chain |
D |
| residue |
48 |
| type |
catalytic |
| sequence |
D
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
10)
|
chain |
D |
| residue |
50 |
| type |
catalytic |
| sequence |
S
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
11)
|
chain |
D |
| residue |
52 |
| type |
catalytic |
| sequence |
D
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
12)
|
chain |
D |
| residue |
59 |
| type |
catalytic |
| sequence |
N
|
| description |
203
|
| source |
MCSA : MCSA2
|
|
|
13)
|
chain |
C |
| residue |
76-94 |
| type |
prosite |
| sequence |
CNIPCSALLSSDITASVNC
|
| description |
GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnipCsaLlssDItasvnC
|
| source |
prosite : PS00128
|
|
|
14)
|
chain |
C |
| residue |
52 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
15)
|
chain |
D |
| residue |
35 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
16)
|
chain |
D |
| residue |
52 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
17)
|
chain |
C |
| residue |
35 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
18)
|
chain |
D |
| residue |
101 |
| type |
BINDING |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
19)
|
chain |
C |
| residue |
101 |
| type |
BINDING |
| sequence |
D
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|