eF-site ID 6cs2-ABCD
PDB Code 6cs2
Chain A, B, C, D
Title SARS Spike Glycoprotein - human ACE2 complex, Stabilized variant, all ACE2-bound particles
Classification viral protein/hydrolase
Compound Spike glycoprotein,Fibritin
Source (ACE2_HUMAN)
Sequence A:  RCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQD
LFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNV
VRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPF
FAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSG
NFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLK
PIFKLPLGINITNFRAILTAFSPIWGTSAAAYFVGYLKPT
TFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIY
QTSNFRVVPSGDVVRFPNLSTDLIKNQCVNFNFNGLTGTG
VLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPC
AFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLT
PAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGI
CASYHTVKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISI
TTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQ
LNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNF
SQILPDPLKPTKRSFIEDLLFNKVQYGECLGDLICAQKFN
GLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQI
PFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQE
SLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSV
LNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAA
EIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAA
PHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFV
FNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNT
VYDPLQPELDS
B:  RCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQD
LFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNV
VRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPF
FAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSG
NFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLK
PIFKLPLGINITNFRAILTAFSPIWGTSAAAYFVGYLKPT
TFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIY
QTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAW
ERKKISNCVADYSVLYNSTFFSTFKCYATKLNDLCFSNVY
ADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAW
NTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPD
GKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFET
VCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQ
QFGRDVSDFTDSVRDPKTSEILDISPCAFGGVSVITPGTN
ASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVF
QTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVQKSIVA
YTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKT
SVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQ
DRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTK
RSFIEDLLFNKVTQYGECLLICAQKFNGLTVLPPLLTDDM
IAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGI
GVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQ
DVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDPPEA
EVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKM
SECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVP
SQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNF
FSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPEL
C:  RCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQD
LFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNV
VRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPF
FAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSG
NFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLK
PIFKLPLGINITNFRAILTAFSPIWGTSAAAYFVGYLKPT
TFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIY
QTSNFRVVPSGDVVRFPNLSTDLIKNQCVNFNFNGLTGTG
VLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPC
AFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLT
PAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGI
CASYHTVQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSIS
ITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCT
QLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFN
FSQILPDPLKPTKRSFIEDLLFNKVTQYGECLGDLICAQK
FNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAAL
QIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQI
QESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAIS
SVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIR
AAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQ
AAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGV
FVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIIN
NTVYDPLQPELDS
D:  STIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEEN
VQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQ
ALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNP
QECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRP
LYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYS
RGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISP
IGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMV
DQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGN
VQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGH
IQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHL
KSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEK
WRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYC
DPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGP
LHKCDISNSTEAGQKLFNMLRLGK
Description (1)  Spike glycoprotein,Envelope glycoprotein, Angiotensin-converting enzyme 2 (E.C.3.4.17.23)


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

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

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

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

6) 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

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

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

9) 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

10) 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

11) 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

12) 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

13) 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

14) 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

15) 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

16) 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

17) chain A
residue 797
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 797
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
source Swiss-Prot : SWS_FT_FI1

19) chain C
residue 797
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402
source Swiss-Prot : SWS_FT_FI1

20) 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

21) chain A
residue 318
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 589
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 602
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 691
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 699
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 783
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 1056
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 1080
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 65
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 1116
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 29
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 65
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 73
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 109
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 118
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 119
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 73
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 158
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 227
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

40) chain B
residue 269
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 318
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 330
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 357
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 589
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 602
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

46) chain B
residue 691
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 699
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 109
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 783
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 1056
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 1080
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 1116
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

53) chain C
residue 29
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

54) chain C
residue 65
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

55) chain C
residue 73
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 118
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

57) chain C
residue 109
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

58) chain C
residue 118
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

59) chain C
residue 119
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

60) chain C
residue 158
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

61) chain C
residue 227
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

62) chain C
residue 269
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

63) chain C
residue 318
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

64) chain C
residue 589
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

65) chain A
residue 119
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

66) chain C
residue 602
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

67) chain C
residue 691
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

68) chain C
residue 699
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

69) chain C
residue 783
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

70) chain C
residue 1056
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

71) chain C
residue 1080
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

72) chain C
residue 1116
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

73) chain A
residue 158
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

74) chain A
residue 227
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

75) chain A
residue 269
type ACT_SITE
sequence N
description Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895
source Swiss-Prot : SWS_FT_FI2

76) chain D
residue 371-380
type prosite
sequence TAHHEMGHIQ
description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ
source prosite : PS00142


Display surface

Download
Links