eF-site ID 7kj4-ABCDEF
PDB Code 7kj4
Chain A, B, C, D, E, F
Title SARS-CoV-2 Spike Glycoprotein with three 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
NNATNVVIKVCEFQFCNDPFNNCTFEYVSFKNLREFVFKN
YFKIYSKHTPINDLPQGFSALEPLVDLPIGINITRFQTLL
AAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCT
LKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVF
NATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGV
SPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYN
YKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLK
PFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNG
VGYQPYRVVVLSFATVCGPKKSTNLVKNKCVNFNFNGLTG
TGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDIT
PCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVNVFQTRAG
CLIGAEHVNNSYECDIPIGAGICASYQTSQSIIAYTMSLG
AENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTM
YICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQE
VFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIED
LLFNKVTKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGW
TFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQ
FNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQL
SSNFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQT
YVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKG
YHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGK
AHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNC
DVVIGIVNNTVYDPLQPELDS
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
F:  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 371-380
type prosite
sequence TAHHEMGHIQ
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
source prosite : PS00142

2) 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

3) 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

4) 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

5) 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

6) 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

7) 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

8) 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

9) 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

10) 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

11) 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

12) 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

13) chain F
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

14) 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

15) 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

16) 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

17) 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

18) 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

19) chain F
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

20) 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

21) 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

22) 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

23) 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

24) 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

25) 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

26) chain F
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

27) chain F
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

28) chain F
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

29) chain D
residue 273
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

30) chain B
residue 1074
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

31) chain C
residue 61
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

32) chain C
residue 122
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

33) chain C
residue 717
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

34) chain C
residue 801
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

35) chain C
residue 1074
type BINDING
sequence N
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

36) chain D
residue 345
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

37) chain D
residue 515
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

38) chain E
residue 273
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

39) chain E
residue 345
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

40) chain E
residue 515
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

41) chain F
residue 273
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

42) chain F
residue 345
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

43) chain F
residue 515
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI4

44) 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

45) 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

46) 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

47) 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

48) 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

49) 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

50) chain F
residue 374
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5

51) chain F
residue 378
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5

52) chain F
residue 402
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI5

53) chain D
residue 53
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

54) chain B
residue 331
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

55) chain B
residue 343
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

56) chain B
residue 616
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

57) chain B
residue 657
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

58) chain B
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

59) chain C
residue 165
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

60) chain C
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

61) chain C
residue 331
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

62) chain C
residue 343
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

63) chain C
residue 616
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

64) chain D
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

65) chain C
residue 657
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

66) chain C
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

67) chain E
residue 53
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

68) chain E
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

69) chain F
residue 53
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

70) chain F
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

71) chain A
residue 1098
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

72) chain B
residue 165
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

73) chain B
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI6

74) chain D
residue 103
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

75) chain D
residue 432
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

76) chain E
residue 103
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

77) chain E
residue 432
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

78) chain F
residue 103
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

79) chain F
residue 432
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895
source Swiss-Prot : SWS_FT_FI8

80) 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

81) 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

82) chain F
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

83) 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

84) 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

85) chain F
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


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