eF-site ID 2vum-ABCDEFGHIJKLM
PDB Code 2vum
Chain A, B, C, D, E, F, G, H, I, J, K, L, M
Title Alpha-amanitin inhibited complete RNA polymerase II elongation complex
Classification TRANSFERASE
Compound DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1
Source ORGANISM_COMMON: BAKERS' YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL
VSRGGCGNTQPTIRKDGLKLVGSWKDEPELRVLSTEEILN
IFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPS
ISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAI
EEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARL
KGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKS
IAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDS
GDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPS
LHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNL
HVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLC
GIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPK
PLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIID
GQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNI
QKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKK
VLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKA
GRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQS
VEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLT
PQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIM
VHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGS
DAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLL
DEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQ
TFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQN
AQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNI
EAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLNTFHVTSG
VPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSA
IEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQ
QSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVI
WSEDNDEKLIIRCRVVAEEDHMLKKIENTMLENITLRGVE
NIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVM
TVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIA
SDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGAL
MRCSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIG
TGAFDVMIDEESLVKYMP
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLN
RYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEG
QACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYV
PHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDIN
PEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKE
LKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEE
SILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEIHP
SMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNY
NVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAIV
AIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKK
YGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRV
SGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTTNQ
DGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRRED
MPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALS
GNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTG
KKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQP
VEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDAF
RVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPY
AAKLLFQELMAMNITPRLYTDRSRDF
C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
D:  STSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGE
EEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKELE
SIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAVI
QLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKISD
DELERILKELSNLETLY
E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVDL
G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG
KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK
PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT
FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI
GSIKEDYLGAI
H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY
DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN
NLKQENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
M:  NXXXGIGX
Description


Functional site

1) chain A
residue 107
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

2) chain A
residue 108
type
sequence M
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

3) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

4) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

5) chain A
residue 166
type
sequence G
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

6) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC1

7) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC2

8) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC2

9) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC2

10) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC2

11) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC3

12) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC3

13) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC3

14) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4

15) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4

16) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4

17) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4

18) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5

19) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5

20) chain C
residue 91
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5

21) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5

22) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5

23) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6

24) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6

25) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6

26) chain I
residue 32
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6

27) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7

28) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7

29) chain I
residue 106
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7

30) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8

31) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8

32) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8

33) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8

34) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9

35) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9

36) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9

37) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9

38) chain A
residue 723
type
sequence N
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

39) chain A
residue 726
type
sequence R
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

40) chain A
residue 759
type
sequence A
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

41) chain A
residue 760
type
sequence Q
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

42) chain A
residue 764
type
sequence C
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

43) chain A
residue 765
type
sequence V
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

44) chain A
residue 766
type
sequence G
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

45) chain A
residue 767
type
sequence Q
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

46) chain A
residue 768
type
sequence Q
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

47) chain A
residue 769
type
sequence S
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

48) chain A
residue 772
type
sequence G
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

49) chain A
residue 819
type
sequence G
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

50) chain A
residue 820
type
sequence G
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

51) chain A
residue 822
type
sequence E
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

52) chain A
residue 1085
type
sequence H
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

53) chain B
residue 763
type
sequence Q
description BINDING SITE FOR CHAIN M OF ALPHA-AMANITIN
source : BC1

54) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5

55) chain I
residue 75
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
source Swiss-Prot : SWS_FT_FI4

56) chain I
residue 78
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
source Swiss-Prot : SWS_FT_FI4

57) chain I
residue 103
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
source Swiss-Prot : SWS_FT_FI4

58) chain I
residue 106
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
source Swiss-Prot : SWS_FT_FI4

59) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1

60) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1

61) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1

62) chain A
residue 1085
type catalytic
sequence H
description 788
source MCSA : MCSA1

63) chain M
residue 4
type CROSSLNK
sequence X
description 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) => ECO:0000305
source Swiss-Prot : SWS_FT_FI3

64) chain M
residue 8
type CROSSLNK
sequence X
description 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) => ECO:0000305
source Swiss-Prot : SWS_FT_FI3

65) chain I
residue 29
type CROSSLNK
sequence C
description 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) => ECO:0000305
source Swiss-Prot : SWS_FT_FI3

66) chain I
residue 32
type CROSSLNK
sequence C
description 2'-cysteinyl-6'-hydroxytryptophan sulfoxide (Trp-Cys) => ECO:0000305
source Swiss-Prot : SWS_FT_FI3

67) chain J
residue 2-11
type prosite
sequence IVPVRCFSCG
description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG
source prosite : PS01112

68) chain F
residue 86-100
type prosite
sequence TKYERARILGTRALQ
description RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARiLGtRAlQ
source prosite : PS01111

69) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466

70) chain I
residue 6-32
type prosite
sequence FCRDCNNMLYPREDKENNRLLFECRTC
description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCrDCNNMLypredkennrllfeCrtC
source prosite : PS01030

71) chain C
residue 31-71
type prosite
sequence NSLRRVMIAEIPTLAIDSVEVETNTTVLADEFIAHRLGLI
P
description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSLRRvmiaeiptlAidsVevetNtTvlaDEfIAhRLGLIP
source prosite : PS00446

72) chain E
residue 147-160
type prosite
sequence HELVPKHIRLSSDE
description RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPKHirLssDE
source prosite : PS01110

73) chain K
residue 35-66
type prosite
sequence FEKEDHTLGNLIRAELLNDRKVLFAAYKVEHP
description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. FekEdHTLgNlIraeLlndrkVlfaaYkveHP
source prosite : PS01154

74) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166

75) chain M
residue 3
type MOD_RES
sequence X
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

76) chain A
residue 483
type MOD_RES
sequence D
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

77) chain A
residue 485
type MOD_RES
sequence D
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

78) chain J
residue 10
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

79) chain J
residue 45
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

80) chain J
residue 46
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

81) chain A
residue 107
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

82) chain A
residue 110
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

83) chain A
residue 148
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

84) chain A
residue 167
type MOD_RES
sequence C
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

85) chain A
residue 481
type MOD_RES
sequence D
description (3R,4S)-4-hydroxyisoleucine; in form gamma-amanitin => ECO:0000269|PubMed:11805306
source Swiss-Prot : SWS_FT_FI1

86) chain M
residue 2
type MOD_RES
sequence X
description 4-hydroxyproline => ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:363352, ECO:0000269|PubMed:4865716
source Swiss-Prot : SWS_FT_FI2

87) chain L
residue 34
type MOD_RES
sequence C
description 4-hydroxyproline => ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:363352, ECO:0000269|PubMed:4865716
source Swiss-Prot : SWS_FT_FI2

88) chain L
residue 48
type MOD_RES
sequence C
description 4-hydroxyproline => ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:363352, ECO:0000269|PubMed:4865716
source Swiss-Prot : SWS_FT_FI2

89) chain L
residue 51
type MOD_RES
sequence C
description 4-hydroxyproline => ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:363352, ECO:0000269|PubMed:4865716
source Swiss-Prot : SWS_FT_FI2

90) chain B
residue 1185
type MOD_RES
sequence C
description 4-hydroxyproline => ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:363352, ECO:0000269|PubMed:4865716
source Swiss-Prot : SWS_FT_FI2


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