|
eF-site ID
|
1c74-A |
PDB Code
|
1c74 |
Chain
|
A |
|
click to enlarge
|
|
Title
|
Structure of the double mutant (K53,56M) of phospholipase A2 |
Classification
|
HYDROLASE |
Compound
|
PHOSPHOLIPASE A2 |
Source
|
Bos taurus (Bovine) (PA21B_BOVIN) |
|
Sequence
|
A: |
ALWQFNGMIKCKIPSSEPLLDFNNYGCYCGLGGSGTPVDD
LDRCCQTHDNCYMQAMKLDSCKVLVDNPYTNNYSYSCSNN
EITCSSENNACEAFICNCDRNAAICFSKVPYNKEHKNLDK
KNC
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
28 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE CA A 124
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
30 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE CA A 124
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
32 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE CA A 124
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
49 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE CA A 124
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
44-51 |
type |
prosite |
sequence |
CCQTHDNC
|
description |
PA2_HIS Phospholipase A2 histidine active site. CCQtHDnC
|
source |
prosite : PS00118
|
|
6)
|
chain |
A |
residue |
95-105 |
type |
prosite |
sequence |
ICNCDRNAAIC
|
description |
PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC
|
source |
prosite : PS00119
|
|
7)
|
chain |
A |
residue |
48 |
type |
ACT_SITE |
sequence |
H
|
description |
ACT_SITE => ECO:0000269|PubMed:7464926
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
8)
|
chain |
A |
residue |
99 |
type |
ACT_SITE |
sequence |
D
|
description |
ACT_SITE => ECO:0000269|PubMed:7464926
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
9)
|
chain |
A |
residue |
28 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
A |
residue |
30 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
A |
residue |
32 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
12)
|
chain |
A |
residue |
49 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:10089353, ECO:0000269|PubMed:7265241, ECO:0000269|PubMed:9115986, ECO:0007744|PDB:1BP2, ECO:0007744|PDB:1KVW, ECO:0007744|PDB:1MKS
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|