eF-site ID
|
4mnq-ABCDE |
PDB Code
|
4mnq |
Chain
|
A, B, C, D, E |
|
click to enlarge
|
|
Title
|
TCR-peptide specificity overrides affinity enhancing TCR-MHC interactions |
Classification
|
IMMUNE SYSTEM |
Compound
|
HLA class I histocompatibility antigen, A-2 alpha chain |
Source
|
Homo sapiens (Human) (TRBC1_HUMAN) |
|
Sequence
|
A: |
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDA
ASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGT
LRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYL
EGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEAT
LRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
|
B: |
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
|
C: |
ILAKFLHWL
|
D: |
IQVEQSPPDLILQEGANSTLRCNFSDSVNNLWWFHQNPWG
QLINLFYIPSGTKQNGRLSATTVATERYSLLYISSSQTTD
SGVYFCAVDSATALPYGYIFGTGTRLKVLANIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVL
DMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPS
|
E: |
AGVTQTPKFQVLKTGQSMTLQCAQDMNHEYMSWYRQDPGM
GLRLIHYSIHPEYTDQGEVPNGYNVSRSTTEDFPLRLLSA
APSQTSVYFCASSYQGTEAFFGQGTRLTVVEDLNKVFPPE
VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGK
EVHSGVCTDPQPLKEQPALNDSRYALSSRLRVSATFWQDP
RNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRAD
|
|
Description
|
(1) |
HLA class I histocompatibility antigen, A-2 alpha chain, Beta-2-microglobulin, Telomerase reverse transcriptase (E.C.2.7.7.49), Uncharacterized protein, T-cell receptor, sp3.4 alpha chain, V_segment translation product, T-cell receptor beta-1 chain C region
|
|
|
|
1)
|
chain |
A |
residue |
35 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GOL A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
40 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE GOL A 301
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
41 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE GOL A 301
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
42 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE GOL A 301
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
46 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE GOL A 301
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
128 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE EDO A 302
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
129 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE EDO A 302
|
source |
: AC2
|
|
8)
|
chain |
D |
residue |
164 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE EDO E 301
|
source |
: AC3
|
|
9)
|
chain |
E |
residue |
163 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE EDO E 301
|
source |
: AC3
|
|
10)
|
chain |
E |
residue |
164 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE EDO E 301
|
source |
: AC3
|
|
11)
|
chain |
E |
residue |
165 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE EDO E 301
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
257-263 |
type |
prosite |
sequence |
YTCHVQH
|
description |
IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH
|
source |
prosite : PS00290
|
|
13)
|
chain |
B |
residue |
78-84 |
type |
prosite |
sequence |
YACRVNH
|
description |
IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCHVQH
|
source |
prosite : PS00290
|
|
14)
|
chain |
E |
residue |
65 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
73 |
type |
CARBOHYD |
sequence |
T
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
A |
residue |
84 |
type |
CARBOHYD |
sequence |
Y
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
143 |
type |
CARBOHYD |
sequence |
T
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
A |
residue |
146 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
19)
|
chain |
A |
residue |
171 |
type |
CARBOHYD |
sequence |
Y
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
20)
|
chain |
E |
residue |
180 |
type |
CARBOHYD |
sequence |
L
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
21)
|
chain |
A |
residue |
159 |
type |
CARBOHYD |
sequence |
Y
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
22)
|
chain |
B |
residue |
19 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
B |
residue |
41 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
24)
|
chain |
B |
residue |
48 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
25)
|
chain |
B |
residue |
58 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
26)
|
chain |
B |
residue |
91 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
27)
|
chain |
B |
residue |
94 |
type |
CARBOHYD |
sequence |
K
|
description |
N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7918443
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
28)
|
chain |
A |
residue |
86 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
|
source |
Swiss-Prot : SWS_FT_FI4
|
|