eF-site ID 7kj3-ABCDE
PDB Code 7kj3
Chain A, B, C, D, E
Title SARS-CoV-2 Spike Glycoprotein with two ACE2 Bound
Classification VIRAL PROTEIN/HYDROLASE
Compound Spike glycoprotein
Source (ACE2_HUMAN)
Sequence A:  AYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFH
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIV
NNATNVVIKVCEFQFCNDPFNNCTFEYVSFKNLREFVFKN
YFKIYSKHTPINDLPQGFSALEPLVDLPIGINITRFQTLL
AAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCT
LKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVF
NATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGV
SPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYN
YKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLK
PFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNG
VGYQPYRVVVLSFATVCGPKKSTNLVKNKCVNFNFNGLTG
TGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDIT
PCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVNVFQTRAG
CLIGAEHVNNSYECDIPIGAGICASYQTSQSIIAYTMSLG
AENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTM
YICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQE
VFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIED
LLFNKVTKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGW
TFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQ
FNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQL
SSNFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQT
YVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKG
YHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGK
AHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNC
DVVIGIVNNTVYDPLQPELDS
B:  AYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFH
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIV
NNATNVVIKVCEFQFCNDPFNNCTFEYVSFKNLREFVFKN
YFKIYSKHTPINDLPQGFSALEPLVDLPIGINITRFQTLL
AAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCT
LKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVF
NATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGV
SPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYN
YKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLK
PFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNG
VGYQPYRVVVLSFATVCGPKKSTNLVKNKCVNFNFNGLTG
TGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDIT
PCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVNVFQTRAG
CLIGAEHVNNSYECDIPIGAGICASYQTSQSIIAYTMSLG
AENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTM
YICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQE
VFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIED
LLFNKVTKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGW
TFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQ
FNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQL
SSNFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQT
YVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKG
YHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGK
AHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNC
DVVIGIVNNTVYDPLQPELDS
C:  AYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFH
NPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIV
NNATNVVIKVCEFQFCNDPFLGVNCTFEYVSFKNLREFVF
KNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGIN
ITRFQTLLAYYVGYLQPRTFLLKYNENGTITDAVDCALDP
LSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNL
CPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFS
TFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQT
GKIADYNYKLPDDFTGCVIAWNSNNLDSKNYNYLYRKPFE
RDISTPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVC
GPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQF
GRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTS
NQVAVLYQDVNCTEVNVFQTRAGCLIGAEHVNNSYECDIP
IGAGICASYQTQSIIAYTMSLGAENSVAYSNNSIAIPTNF
TISVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGS
FCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFG
GFNFSQILPDPSKPSKRSFIEDLLFNKVTNGLTVLPPLLT
DEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRF
NGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALG
KLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDP
PEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAA
TKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVT
YVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQ
RNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELD
S
D:  IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ
NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQAL
QQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQE
CLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY
EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRG
QLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIG
CLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ
AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQ
KAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQ
YDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS
IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWR
WMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDP
ASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH
KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMN
VRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPY
E:  IEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ
NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQAL
QQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQE
CLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY
EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRG
QLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIG
CLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ
AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQ
KAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQ
YDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS
IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWR
WMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDP
ASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH
KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMN
VRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPY
Description (1)  Spike glycoprotein


Functional site
1) chain D
residue 273
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
2) chain B
residue 1074
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
3) chain C
residue 61
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
4) chain C
residue 122
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
5) chain C
residue 717
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
6) chain C
residue 801
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
7) chain C
residue 1074
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
8) chain D
residue 345
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
9) chain D
residue 515
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
10) chain E
residue 273
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
11) chain E
residue 345
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
12) chain E
residue 515
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
13) chain B
residue 122
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
14) chain B
residue 717
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
15) chain B
residue 801
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4
16) chain D
residue 169
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
17) chain D
residue 477
type BINDING
sequence W
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
18) chain D
residue 481
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
19) chain E
residue 169
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
20) chain E
residue 477
type BINDING
sequence W
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
21) chain E
residue 481
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774
source Swiss-Prot : SWS_FT_FI3
22) chain D
residue 374
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
23) chain D
residue 378
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
24) chain D
residue 402
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
25) chain E
residue 374
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
26) chain E
residue 378
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
27) chain E
residue 402
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5
28) chain D
residue 375
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
source Swiss-Prot : SWS_FT_FI1
29) chain E
residue 375
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
source Swiss-Prot : SWS_FT_FI1
30) chain D
residue 505
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2
31) chain E
residue 505
type ACT_SITE
sequence H
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2
32) chain C
residue 815
type ACT_SITE
sequence R
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2
33) chain D
residue 371-380
type prosite
sequence TAHHEMGHIQ
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
source prosite : PS00142
34) chain A
residue 1134
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI12
35) chain B
residue 1134
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI12
36) chain C
residue 1134
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI12
37) chain A
residue 676
type CARBOHYD
sequence T
description O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
source Swiss-Prot : SWS_FT_FI11
38) chain B
residue 676
type CARBOHYD
sequence T
description O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
source Swiss-Prot : SWS_FT_FI11
39) chain C
residue 676
type CARBOHYD
sequence T
description O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
source Swiss-Prot : SWS_FT_FI11
40) chain A
residue 603
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI10
41) chain B
residue 603
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI10
42) chain C
residue 603
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
source Swiss-Prot : SWS_FT_FI10
43) chain D
residue 103
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8
44) chain D
residue 432
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8
45) chain E
residue 103
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8
46) chain E
residue 432
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8
47) chain D
residue 546
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI9
48) chain E
residue 546
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI9
49) chain C
residue 325
type CARBOHYD
sequence S
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI9
50) chain D
residue 53
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
51) chain B
residue 331
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
52) chain B
residue 343
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
53) chain B
residue 616
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
54) chain B
residue 657
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
55) chain B
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
56) chain C
residue 165
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
57) chain C
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
58) chain C
residue 331
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
59) chain C
residue 343
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
60) chain C
residue 616
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
61) chain D
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
62) chain C
residue 657
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
63) chain C
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
64) chain E
residue 53
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
65) chain E
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
66) chain A
residue 616
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
67) chain A
residue 657
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
68) chain A
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
69) chain B
residue 165
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
70) chain B
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6
71) chain D
residue 90
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7
72) chain E
residue 90
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7
73) chain B
residue 234
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7
74) chain B
residue 709
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7
75) chain C
residue 234
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7
76) chain C
residue 709
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337
source Swiss-Prot : SWS_FT_FI7

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