|
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eF-site ID
|
5at1-C |
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PDB Code
|
5at1 |
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Chain
|
C |
|
click to enlarge
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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 |
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Classification
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TRANSFERASE (CARBAMOYL-P,ASPARTATE) |
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Compound
|
ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN |
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Source
|
null (PYRI_ECOLI) |
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Sequence
|
C: |
ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK
HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG
NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT
PHAWYFQQAGNGIFARQALLALVLNRDLVL
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Description
|
(1) |
ASPARTATE CARBAMOYLTRANSFERASE (ASPARTATE TRANSCARBAMYLASE) (T STATE) (E.C.2.1.3.2) COMPLEX WITH CYTIDINE 5-PRIME-TRIPHOSPHATE (CTP)
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Functional site
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1)
|
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
|
|
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2)
|
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
|
|
|
3)
|
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
|
|
|
4)
|
chain |
C |
| residue |
55 |
| type |
catalytic |
| sequence |
T
|
| description |
405
|
| source |
MCSA : MCSA2
|
|
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5)
|
chain |
C |
| residue |
56 |
| type |
catalytic |
| sequence |
R
|
| description |
405
|
| source |
MCSA : MCSA2
|
|
|
6)
|
chain |
C |
| residue |
85 |
| type |
catalytic |
| sequence |
G
|
| description |
405
|
| source |
MCSA : MCSA2
|
|
|
7)
|
chain |
C |
| residue |
106 |
| type |
catalytic |
| sequence |
H
|
| description |
405
|
| source |
MCSA : MCSA2
|
|
|
8)
|
chain |
C |
| residue |
135 |
| type |
catalytic |
| sequence |
P
|
| description |
405
|
| source |
MCSA : MCSA2
|
|
|
9)
|
chain |
C |
| residue |
106 |
| type |
BINDING |
| sequence |
H
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
10)
|
chain |
C |
| residue |
135 |
| type |
BINDING |
| sequence |
P
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
11)
|
chain |
C |
| residue |
138 |
| type |
BINDING |
| sequence |
T
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
12)
|
chain |
C |
| residue |
268 |
| type |
BINDING |
| sequence |
P
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
13)
|
chain |
C |
| residue |
269 |
| type |
BINDING |
| sequence |
R
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
14)
|
chain |
C |
| residue |
56 |
| type |
BINDING |
| sequence |
R
|
| description |
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|