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eF-site ID
|
1kct-A |
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PDB Code
|
1kct |
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Chain
|
A |
|
click to enlarge
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Title
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ALPHA1-ANTITRYPSIN |
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Classification
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SERINE PROTEASE INHIBITOR |
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Compound
|
ALPHA1-ANTITRYPSIN |
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Source
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Homo sapiens (Human) (A1AT_HUMAN) |
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Sequence
|
A: |
HPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIAA
AFAMLSLGAKGDTHDEILEGLNFNLTEIPEAQIHEGFQEL
LRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYH
SEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRD
TVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVP
MMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGK
LQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDL
KSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLT
IDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNT
KSPLFMGKVVNPTQK
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Description
|
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Functional site
|
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1)
|
chain |
A |
| residue |
358 |
| type |
|
| sequence |
M
|
| description |
REACTIVE SITE IN INHIBITORY LOOP.
|
| source |
: P1
|
|
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2)
|
chain |
A |
| residue |
358 |
| type |
SITE |
| sequence |
M
|
| description |
Reactive bond
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| source |
Swiss-Prot : SWS_FT_FI3
|
|
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3)
|
chain |
A |
| residue |
232 |
| type |
MOD_RES |
| sequence |
C
|
| description |
S-cysteinyl cysteine
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
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4)
|
chain |
A |
| residue |
328 |
| type |
SITE |
| sequence |
K
|
| description |
(Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur => ECO:0000269|PubMed:3533918
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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5)
|
chain |
A |
| residue |
330 |
| type |
SITE |
| sequence |
S
|
| description |
(Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases => ECO:0000269|PubMed:3533918
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
6)
|
chain |
A |
| residue |
359 |
| type |
MOD_RES |
| sequence |
S
|
| description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
7)
|
chain |
A |
| residue |
83 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
8)
|
chain |
A |
| residue |
247 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
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9)
|
chain |
A |
| residue |
46 |
| type |
CARBOHYD |
| sequence |
N
|
| description |
N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
10)
|
chain |
A |
| residue |
364-374 |
| type |
prosite |
| sequence |
VKFNKPFVFLM
|
| description |
SERPIN Serpins signature. VKFNKPFVFlM
|
| source |
prosite : PS00284
|
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