|
eF-site ID
|
2p6b-C |
PDB Code
|
2p6b |
Chain
|
C |
|
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|
|
Title
|
Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide |
Classification
|
HYDROLASE/HYDROLASE REGULATOR |
Compound
|
PVIVIT 14-mer Peptide |
Source
|
(2P6B) |
|
Sequence
|
C: |
TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKE
GRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHG
QFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYL
WALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSER
VYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTV
RGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRK
SQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQ
FNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLN
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
C |
residue |
118 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE ZN C 512
|
source |
: AC8
|
|
2)
|
chain |
C |
residue |
150 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE ZN C 512
|
source |
: AC8
|
|
3)
|
chain |
C |
residue |
199 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN C 512
|
source |
: AC8
|
|
4)
|
chain |
C |
residue |
281 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN C 512
|
source |
: AC8
|
|
5)
|
chain |
C |
residue |
90 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE FE C 513
|
source |
: AC9
|
|
6)
|
chain |
C |
residue |
92 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE FE C 513
|
source |
: AC9
|
|
7)
|
chain |
C |
residue |
118 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE FE C 513
|
source |
: AC9
|
|
8)
|
chain |
C |
residue |
92 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
9)
|
chain |
C |
residue |
118 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
10)
|
chain |
C |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
11)
|
chain |
C |
residue |
150 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
12)
|
chain |
C |
residue |
151 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
13)
|
chain |
C |
residue |
254 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
14)
|
chain |
C |
residue |
281 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE PO4 C 514
|
source |
: BC1
|
|
15)
|
chain |
C |
residue |
90 |
type |
catalytic |
sequence |
D
|
description |
406
|
source |
MCSA : MCSA2
|
|
16)
|
chain |
C |
residue |
281 |
type |
catalytic |
sequence |
H
|
description |
406
|
source |
MCSA : MCSA2
|
|
17)
|
chain |
C |
residue |
92 |
type |
catalytic |
sequence |
H
|
description |
406
|
source |
MCSA : MCSA2
|
|
18)
|
chain |
C |
residue |
118 |
type |
catalytic |
sequence |
D
|
description |
406
|
source |
MCSA : MCSA2
|
|
19)
|
chain |
C |
residue |
121 |
type |
catalytic |
sequence |
D
|
description |
406
|
source |
MCSA : MCSA2
|
|
20)
|
chain |
C |
residue |
122 |
type |
catalytic |
sequence |
R
|
description |
406
|
source |
MCSA : MCSA2
|
|
21)
|
chain |
C |
residue |
150 |
type |
catalytic |
sequence |
N
|
description |
406
|
source |
MCSA : MCSA2
|
|
22)
|
chain |
C |
residue |
151 |
type |
catalytic |
sequence |
H
|
description |
406
|
source |
MCSA : MCSA2
|
|
23)
|
chain |
C |
residue |
199 |
type |
catalytic |
sequence |
H
|
description |
406
|
source |
MCSA : MCSA2
|
|
24)
|
chain |
C |
residue |
254 |
type |
catalytic |
sequence |
R
|
description |
406
|
source |
MCSA : MCSA2
|
|
25)
|
chain |
C |
residue |
199 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
26)
|
chain |
C |
residue |
281 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
27)
|
chain |
C |
residue |
224 |
type |
MOD_RES |
sequence |
Y
|
description |
3'-nitrotyrosine => ECO:0000250|UniProtKB:P63328
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
|
|