|
|
eF-site ID
|
1sqm-A |
|
PDB Code
|
1sqm |
|
Chain
|
A |
|
click to enlarge
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Title
|
STRUCTURE OF [R563A] LEUKOTRIENE A4 HYDROLASE |
|
Classification
|
HYDROLASE |
|
Compound
|
LEUKOTRIENE A-4 HYDROLASE |
|
Source
|
(LKHA4_HUMAN) |
|
|
Sequence
|
A: |
PEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAAL
TVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQS
YKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTP
EQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEV
SVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCY
LIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESM
LKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTP
TLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGH
TVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETH
PFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGP
EIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLN
QVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKE
DDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRM
QEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATE
QGAMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTA
MLVGKDLKVD
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Description
|
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Functional site
|
|
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1)
|
chain |
A |
| residue |
295 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 1001
|
| source |
: AC1
|
|
|
2)
|
chain |
A |
| residue |
299 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 1001
|
| source |
: AC1
|
|
|
3)
|
chain |
A |
| residue |
318 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ZN A 1001
|
| source |
: AC1
|
|
|
4)
|
chain |
A |
| residue |
47 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE YB A 2001
|
| source |
: AC2
|
|
|
5)
|
chain |
A |
| residue |
481 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE YB A 2001
|
| source |
: AC2
|
|
|
6)
|
chain |
A |
| residue |
344 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
7)
|
chain |
A |
| residue |
347 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
8)
|
chain |
A |
| residue |
348 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
9)
|
chain |
A |
| residue |
501 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
10)
|
chain |
A |
| residue |
504 |
| type |
|
| sequence |
A
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
11)
|
chain |
A |
| residue |
508 |
| type |
|
| sequence |
Q
|
| description |
BINDING SITE FOR RESIDUE IMD A 2002
|
| source |
: AC3
|
|
|
12)
|
chain |
A |
| residue |
269 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
13)
|
chain |
A |
| residue |
271 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
14)
|
chain |
A |
| residue |
295 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
15)
|
chain |
A |
| residue |
296 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
16)
|
chain |
A |
| residue |
299 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
17)
|
chain |
A |
| residue |
318 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
18)
|
chain |
A |
| residue |
383 |
| type |
|
| sequence |
Y
|
| description |
BINDING SITE FOR RESIDUE ACY A 3001
|
| source |
: AC4
|
|
|
19)
|
chain |
A |
| residue |
272 |
| type |
catalytic |
| sequence |
N
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
20)
|
chain |
A |
| residue |
296 |
| type |
catalytic |
| sequence |
E
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
21)
|
chain |
A |
| residue |
297 |
| type |
catalytic |
| sequence |
I
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
22)
|
chain |
A |
| residue |
300 |
| type |
catalytic |
| sequence |
S
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
23)
|
chain |
A |
| residue |
319 |
| type |
catalytic |
| sequence |
G
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
24)
|
chain |
A |
| residue |
376 |
| type |
catalytic |
| sequence |
V
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
25)
|
chain |
A |
| residue |
384 |
| type |
catalytic |
| sequence |
E
|
| description |
166
|
| source |
MCSA : MCSA1
|
|
|
26)
|
chain |
A |
| residue |
292-301 |
| type |
prosite |
| sequence |
VIAHEISHSW
|
| description |
ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHEISHSW
|
| source |
prosite : PS00142
|
|
|
27)
|
chain |
A |
| residue |
73 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
28)
|
chain |
A |
| residue |
337 |
| type |
MOD_RES |
| sequence |
F
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
29)
|
chain |
A |
| residue |
414 |
| type |
MOD_RES |
| sequence |
F
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
30)
|
chain |
A |
| residue |
573 |
| type |
MOD_RES |
| sequence |
D
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
31)
|
chain |
A |
| residue |
297 |
| type |
ACT_SITE |
| sequence |
I
|
| description |
Proton acceptor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
32)
|
chain |
A |
| residue |
384 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Proton donor => ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002, ECO:0000305|PubMed:24591641, ECO:0007744|PDB:1H19
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
33)
|
chain |
A |
| residue |
135 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:18804029
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
34)
|
chain |
A |
| residue |
267 |
| type |
BINDING |
| sequence |
Y
|
| description |
BINDING => ECO:0000269|PubMed:18804029
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
35)
|
chain |
A |
| residue |
564 |
| type |
BINDING |
| sequence |
M
|
| description |
BINDING => ECO:0000269|PubMed:18804029
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
36)
|
chain |
A |
| residue |
272 |
| type |
SITE |
| sequence |
N
|
| description |
Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
37)
|
chain |
A |
| residue |
563 |
| type |
SITE |
| sequence |
A
|
| description |
Pro-Gly-Pro binding => ECO:0000269|PubMed:24591641
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
38)
|
chain |
A |
| residue |
376 |
| type |
SITE |
| sequence |
V
|
| description |
Essential for epoxide hydrolase activity, but not for aminopeptidase activity => ECO:0000269|PubMed:11917124
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
39)
|
chain |
A |
| residue |
379 |
| type |
SITE |
| sequence |
S
|
| description |
Covalently modified during suicide inhibition by leukotrienes => ECO:0000269|PubMed:7667299
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
40)
|
chain |
A |
| residue |
416 |
| type |
MOD_RES |
| sequence |
Y
|
| description |
Phosphoserine => ECO:0000269|PubMed:9395533
|
| source |
Swiss-Prot : SWS_FT_FI10
|
|
|
41)
|
chain |
A |
| residue |
296 |
| type |
BINDING |
| sequence |
E
|
| description |
BINDING => ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:11675384, ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:19618939, ECO:0000269|PubMed:24591641, ECO:0007744|PDB:1GW6, ECO:0007744|PDB:1H19, ECO:0007744|PDB:1HS6, ECO:0007744|PDB:1SQM, ECO:0007744|PDB:2R59, ECO:0007744|PDB:2VJ8, ECO:0007744|PDB:3B7R, ECO:0007744|PDB:3B7S, ECO:0007744|PDB:3B7T, ECO:0007744|PDB:3B7U, ECO:0007744|PDB:3CHO, ECO:0007744|PDB:3CHP, ECO:0007744|PDB:3CHQ, ECO:0007744|PDB:3CHR, ECO:0007744|PDB:3CHS, ECO:0007744|PDB:3FH5, ECO:0007744|PDB:3FH7, ECO:0007744|PDB:3FH8, ECO:0007744|PDB:3FHE, ECO:0007744|PDB:3FTS, ECO:0007744|PDB:3FTU, ECO:0007744|PDB:3FTV, ECO:0007744|PDB:3FTW, ECO:0007744|PDB:3FTX, ECO:0007744|PDB:3FTY, ECO:0007744|PDB:3FTZ, ECO:0007744|PDB:3FU0, ECO:0007744|PDB:3FU3, ECO:0007744|PDB:3FU5, ECO:0007744|PDB:3FU6, ECO:0007744|PDB:3FUD, ECO:0007744|PDB:3FUE, ECO:0007744|PDB:3FUF, ECO:0007744|PDB:3FUH, ECO:0007744|PDB:3FUI, ECO:0007744|PDB:3FUJ, ECO:0007744|PDB:3FUK, ECO:0007744|PDB:3FUL, ECO:0007744|PDB:3FUM, ECO:0007744|PDB:3FUN, ECO:0007744|PDB:3U9W, ECO:0007744|PDB:4DPR, ECO:0007744|PDB:4L2L, ECO:0007744|PDB:4MKT, ECO:0007744|PDB:4MS6, ECO:0007744|PDB:5AEN
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
42)
|
chain |
A |
| residue |
300 |
| type |
BINDING |
| sequence |
S
|
| description |
BINDING => ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:11675384, ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:19618939, ECO:0000269|PubMed:24591641, ECO:0007744|PDB:1GW6, ECO:0007744|PDB:1H19, ECO:0007744|PDB:1HS6, ECO:0007744|PDB:1SQM, ECO:0007744|PDB:2R59, ECO:0007744|PDB:2VJ8, ECO:0007744|PDB:3B7R, ECO:0007744|PDB:3B7S, ECO:0007744|PDB:3B7T, ECO:0007744|PDB:3B7U, ECO:0007744|PDB:3CHO, ECO:0007744|PDB:3CHP, ECO:0007744|PDB:3CHQ, ECO:0007744|PDB:3CHR, ECO:0007744|PDB:3CHS, ECO:0007744|PDB:3FH5, ECO:0007744|PDB:3FH7, ECO:0007744|PDB:3FH8, ECO:0007744|PDB:3FHE, ECO:0007744|PDB:3FTS, ECO:0007744|PDB:3FTU, ECO:0007744|PDB:3FTV, ECO:0007744|PDB:3FTW, ECO:0007744|PDB:3FTX, ECO:0007744|PDB:3FTY, ECO:0007744|PDB:3FTZ, ECO:0007744|PDB:3FU0, ECO:0007744|PDB:3FU3, ECO:0007744|PDB:3FU5, ECO:0007744|PDB:3FU6, ECO:0007744|PDB:3FUD, ECO:0007744|PDB:3FUE, ECO:0007744|PDB:3FUF, ECO:0007744|PDB:3FUH, ECO:0007744|PDB:3FUI, ECO:0007744|PDB:3FUJ, ECO:0007744|PDB:3FUK, ECO:0007744|PDB:3FUL, ECO:0007744|PDB:3FUM, ECO:0007744|PDB:3FUN, ECO:0007744|PDB:3U9W, ECO:0007744|PDB:4DPR, ECO:0007744|PDB:4L2L, ECO:0007744|PDB:4MKT, ECO:0007744|PDB:4MS6, ECO:0007744|PDB:5AEN
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
43)
|
chain |
A |
| residue |
319 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:24591641, ECO:0007744|PDB:1GW6, ECO:0007744|PDB:1H19, ECO:0007744|PDB:1HS6, ECO:0007744|PDB:1SQM, ECO:0007744|PDB:2R59, ECO:0007744|PDB:2VJ8, ECO:0007744|PDB:3B7R, ECO:0007744|PDB:3B7S, ECO:0007744|PDB:3B7T, ECO:0007744|PDB:3B7U, ECO:0007744|PDB:3CHO, ECO:0007744|PDB:3CHP, ECO:0007744|PDB:3CHQ, ECO:0007744|PDB:3CHR, ECO:0007744|PDB:3CHS, ECO:0007744|PDB:3FH5, ECO:0007744|PDB:3FH7, ECO:0007744|PDB:3FH8, ECO:0007744|PDB:3FHE, ECO:0007744|PDB:3FTS, ECO:0007744|PDB:3FTU, ECO:0007744|PDB:3FTV, ECO:0007744|PDB:3FTW, ECO:0007744|PDB:3FTX, ECO:0007744|PDB:3FTY, ECO:0007744|PDB:3FTZ, ECO:0007744|PDB:3FU0, ECO:0007744|PDB:3FU3, ECO:0007744|PDB:3FU5, ECO:0007744|PDB:3FU6, ECO:0007744|PDB:3FUD, ECO:0007744|PDB:3FUE, ECO:0007744|PDB:3FUF, ECO:0007744|PDB:3FUH, ECO:0007744|PDB:3FUI, ECO:0007744|PDB:3FUJ, ECO:0007744|PDB:3FUK, ECO:0007744|PDB:3FUL, ECO:0007744|PDB:3FUM, ECO:0007744|PDB:3FUN, ECO:0007744|PDB:3U9W, ECO:0007744|PDB:4DPR, ECO:0007744|PDB:4L2L, ECO:0007744|PDB:4MKT, ECO:0007744|PDB:4MS6, ECO:0007744|PDB:5AEN
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
|