|
|
eF-site ID
|
6cox-AB |
|
PDB Code
|
6cox |
|
Chain
|
A, B |
|
click to enlarge
|
|
|
Title
|
CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A SELECTIVE INHIBITOR, SC-558 IN I222 SPACE GROUP |
|
Classification
|
OXIDOREDUCTASE |
|
Compound
|
CYCLOOXYGENASE-2 |
|
Source
|
(PGH2_MOUSE) |
|
|
Sequence
|
A: |
ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
|
| B: |
ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
385 |
| type |
|
| sequence |
Y
|
| description |
TYR 385 IS BELIEVED TO BE THE AMINO ACID THAT ABSTRACTS A HYDROGEN ATOM FROM THE SUBSTRATE. IT IS LOCATED CLOSE TO THE HEME. A TYROSINE RADICAL IS FORMED DURING THE COURSE OF THE REACTION.
|
| source |
: CAT
|
|
|
2)
|
chain |
A |
| residue |
530 |
| type |
|
| sequence |
S
|
| description |
SER 530 IS ACETYLATED BY ASPIRIN (AN ACETYL GROUP IS COVALENTLY ATTACHED TO THE PROTEIN WHEN INHIBITED WITH ASPIRIN). THE ACETYLATED SER PREVENTS THE PROPER BINDING OF THE SUBSTRATE IN THE CYCLOOXYGENASE ACTIVE SITE. IT HAS BEEN RECENTLY SHOWN, HOWEVER, THAT ACETYLATION OF CYCLOOXYGENASE-2 RESULTS IN THE FORMATION OF A DIFFERENT PRODUCT (15-HETE).
|
| source |
: ACE
|
|
|
3)
|
chain |
A |
| residue |
388 |
| type |
|
| sequence |
H
|
| description |
HIS 388 IS THE AXIAL LIGAND TO THE HEME.
|
| source |
: HEM
|
|
|
4)
|
chain |
A |
| residue |
120 |
| type |
|
| sequence |
R
|
| description |
ARGININE 120 IS BELIEVED TO ANCHOR THE CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.
|
| source |
: SUB
|
|
|
5)
|
chain |
A |
| residue |
203 |
| type |
catalytic |
| sequence |
Q
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
A |
| residue |
207 |
| type |
catalytic |
| sequence |
H
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
A |
| residue |
384 |
| type |
catalytic |
| sequence |
L
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
8)
|
chain |
A |
| residue |
385 |
| type |
catalytic |
| sequence |
Y
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
9)
|
chain |
A |
| residue |
388 |
| type |
catalytic |
| sequence |
H
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
10)
|
chain |
A |
| residue |
526 |
| type |
catalytic |
| sequence |
G
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
11)
|
chain |
A |
| residue |
530 |
| type |
catalytic |
| sequence |
S
|
| description |
37
|
| source |
MCSA : MCSA1
|
|
|
12)
|
chain |
B |
| residue |
203 |
| type |
catalytic |
| sequence |
Q
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
13)
|
chain |
B |
| residue |
207 |
| type |
catalytic |
| sequence |
H
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
14)
|
chain |
B |
| residue |
384 |
| type |
catalytic |
| sequence |
L
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
15)
|
chain |
B |
| residue |
385 |
| type |
catalytic |
| sequence |
Y
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
16)
|
chain |
B |
| residue |
388 |
| type |
catalytic |
| sequence |
H
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
17)
|
chain |
B |
| residue |
526 |
| type |
catalytic |
| sequence |
G
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
18)
|
chain |
B |
| residue |
530 |
| type |
catalytic |
| sequence |
S
|
| description |
37
|
| source |
MCSA : MCSA2
|
|
|
19)
|
chain |
A |
| residue |
207 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
20)
|
chain |
B |
| residue |
207 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
21)
|
chain |
A |
| residue |
144 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI10
|
|
|
22)
|
chain |
B |
| residue |
144 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI10
|
|
|
23)
|
chain |
A |
| residue |
410 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI11
|
|
|
24)
|
chain |
B |
| residue |
410 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI11
|
|
|
25)
|
chain |
A |
| residue |
385 |
| type |
ACT_SITE |
| sequence |
Y
|
| description |
For cyclooxygenase activity => ECO:0000269|PubMed:20463020
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
26)
|
chain |
B |
| residue |
385 |
| type |
ACT_SITE |
| sequence |
Y
|
| description |
For cyclooxygenase activity => ECO:0000269|PubMed:20463020
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
27)
|
chain |
A |
| residue |
120 |
| type |
BINDING |
| sequence |
R
|
| description |
BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
28)
|
chain |
A |
| residue |
355 |
| type |
BINDING |
| sequence |
Y
|
| description |
BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
29)
|
chain |
B |
| residue |
120 |
| type |
BINDING |
| sequence |
R
|
| description |
BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
30)
|
chain |
B |
| residue |
355 |
| type |
BINDING |
| sequence |
Y
|
| description |
BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
31)
|
chain |
A |
| residue |
388 |
| type |
BINDING |
| sequence |
H
|
| description |
axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
32)
|
chain |
B |
| residue |
388 |
| type |
BINDING |
| sequence |
H
|
| description |
axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
33)
|
chain |
A |
| residue |
530 |
| type |
SITE |
| sequence |
S
|
| description |
Aspirin-acetylated serine
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
34)
|
chain |
B |
| residue |
530 |
| type |
SITE |
| sequence |
S
|
| description |
Aspirin-acetylated serine
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
35)
|
chain |
A |
| residue |
540 |
| type |
MOD_RES |
| sequence |
C
|
| description |
S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
36)
|
chain |
B |
| residue |
540 |
| type |
MOD_RES |
| sequence |
C
|
| description |
S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
37)
|
chain |
A |
| residue |
579 |
| type |
MOD_RES |
| sequence |
S
|
| description |
O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
38)
|
chain |
B |
| residue |
579 |
| type |
MOD_RES |
| sequence |
S
|
| description |
O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
39)
|
chain |
A |
| residue |
68 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
40)
|
chain |
B |
| residue |
68 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
|