eF-site ID 1ant-IL
PDB Code 1ant
Chain I, L

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Title BIOLOGICAL IMPLICATIONS OF A 3 ANGSTROMS STRUCTURE OF DIMERIC ANTITHROMBIN
Classification SERINE PROTEASE INHIBITOR
Compound ANTITHROMBIN
Source Homo sapiens (Human) (ANT3_HUMAN)
Sequence I:  RDIPMNPMCIYRSPEKKATNRRVWELSKANSRFATTFYQH
LADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEV
FKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANR
LFGDKSLTFNETYQDISELVYGAKLQPLDFKENAEQSRAA
INKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLW
KSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE
GTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQ
EWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFS
PEKSKLPGIVAEGRDDLYVSDAFHKAFLEVNEAASTAVVI
AGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGRVANPC
VK
L:  DIPMNPMCIYRSATNRRVWELSKANSRFATTFYQHLADSK
NDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDT
ISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDK
SLTFNETYQDISELVYGAKLQPLDFKENAEQSRAAINKWV
SNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFS
PENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVL
ELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDE
LEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSK
LPGIVAEGRDDLYVSDAFHKAFLEVNEEGSEAAASTAVVI
AGRSLRPFLVFIREVPLNTIIFMGRVANPCVK
Description (1)  ANTITHROMBIN


Functional site

1) chain L
residue 49
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI1

2) chain L
residue 129
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

3) chain L
residue 145
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

4) chain I
residue 49
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI1

5) chain I
residue 129
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

6) chain I
residue 145
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

7) chain L
residue 155
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI7

8) chain I
residue 155
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI7

9) chain L
residue 192
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI8

10) chain I
residue 192
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI8

11) chain L
residue 393
type SITE
sequence R
description Reactive bond => ECO:0000269|PubMed:7238875
source Swiss-Prot : SWS_FT_FI2

12) chain I
residue 393
type SITE
sequence R
description Reactive bond => ECO:0000269|PubMed:7238875
source Swiss-Prot : SWS_FT_FI2

13) chain L
residue 96
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI5

14) chain I
residue 96
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI5

15) chain L
residue 135
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI6

16) chain I
residue 135
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10
source Swiss-Prot : SWS_FT_FI6


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