|
eF-site ID
|
4at1-C |
PDB Code
|
4at1 |
Chain
|
C |
|
click to enlarge
|
|
Title
|
STRUCTURAL CONSEQUENCES OF EFFECTOR BINDING TO THE T STATE OF ASPARTATE CARBAMOYLTRANSFERASE. CRYSTAL STRUCTURES OF THE UNLIGATED AND ATP-, AND CTP-COMPLEXED ENZYMES AT 2.6-ANGSTROMS RESOLUTION |
Classification
|
TRANSFERASE (CARBAMOYL-P,ASPARTATE) |
Compound
|
ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN |
Source
|
Escherichia coli (strain K12) (PYRI_ECOLI) |
|
Sequence
|
C: |
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK
HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG
NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT
PHAWYFQQAGNGIFARQALLALVLNRDLVL
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
C |
residue |
55 |
type |
catalytic |
sequence |
T
|
description |
405
|
source |
MCSA : MCSA2
|
|
2)
|
chain |
C |
residue |
56 |
type |
catalytic |
sequence |
R
|
description |
405
|
source |
MCSA : MCSA2
|
|
3)
|
chain |
C |
residue |
85 |
type |
catalytic |
sequence |
G
|
description |
405
|
source |
MCSA : MCSA2
|
|
4)
|
chain |
C |
residue |
106 |
type |
catalytic |
sequence |
H
|
description |
405
|
source |
MCSA : MCSA2
|
|
5)
|
chain |
C |
residue |
135 |
type |
catalytic |
sequence |
P
|
description |
405
|
source |
MCSA : MCSA2
|
|
6)
|
chain |
C |
residue |
106 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
7)
|
chain |
C |
residue |
135 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
8)
|
chain |
C |
residue |
138 |
type |
BINDING |
sequence |
T
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
9)
|
chain |
C |
residue |
268 |
type |
BINDING |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
chain |
C |
residue |
269 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
11)
|
chain |
C |
residue |
56 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
C |
residue |
85 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
C |
residue |
168 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
C |
residue |
230 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|