eF-site ID
|
4a3g-ABCDEFGHIJKL |
PDB Code
|
4a3g |
Chain
|
A, B, C, D, E, F, G, H, I, J, K, L |
|
|
|
Title
|
RNA Polymerase II initial transcribing complex with a 2nt DNA-RNA hybrid |
Classification
|
TRANSCRIPTION |
Compound
|
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 |
Source
|
ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; |
|
Sequence
|
A: |
GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD
ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG
HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM
RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLV
SRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVL
STEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVP
PPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHN
GAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPV
KSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELD
QVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGA
KYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPV
LFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADF
DGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMG
IVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPT
PAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKD
NGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVC
AKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITET
IAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFL
NEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMS
ACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVEN
SYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLV
KALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQS
LDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGD
LKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRR
IIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRG
KNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAF
DWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTKK
VTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKL
IRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLH
FSLQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKND
LFVIWSEDNDEKLIIRCRVVAEEDHMLKKIENTMLENITL
RGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNL
SEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVY
NVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSN
TGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQM
APIGTGAFDVMIDEESLVKYMP
|
B: |
DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGIKKEK
RIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMINRLLL
CALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKD
IFRYMQRTVELAINAKTITSGLKYALATGNWGEQKKAMSS
RAGVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGL
VCPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEW
GMEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLR
TLRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVE
DDESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLV
EYIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHAT
TFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQ
AMGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRE
LPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFF
RSYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDD
GLIAPGVRVSGEDVIIGKTTPISSKRDASTPLRSTENGIV
DQVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGT
IGITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIEC
LLSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGF
EVMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARG
PMQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKE
RLMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKI
DIYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF
|
C: |
EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
|
D: |
VSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQG
EEEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKEL
ESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAV
IQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKIS
DDELERILKELSNLETLY
|
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
YDPKDALKNACNSIINKLGALKTNFETEWNLQTLA
|
L: |
ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
|
|
Description
|
(1) |
DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, RPB7, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4
|
|
|
|
1)
|
chain |
A |
residue |
107 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
110 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
148 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
167 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2456
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
67 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
69 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
70 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
77 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
80 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 2457
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
481 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
483 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
485 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE MG A 2458
|
source |
: AC3
|
|
13)
|
chain |
B |
residue |
1163 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
14)
|
chain |
B |
residue |
1166 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
15)
|
chain |
B |
residue |
1182 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
16)
|
chain |
B |
residue |
1185 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 2225
|
source |
: AC4
|
|
17)
|
chain |
C |
residue |
86 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
18)
|
chain |
C |
residue |
88 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
19)
|
chain |
C |
residue |
92 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
20)
|
chain |
C |
residue |
95 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 1269
|
source |
: AC5
|
|
21)
|
chain |
I |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
22)
|
chain |
I |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
23)
|
chain |
I |
residue |
29 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
24)
|
chain |
I |
residue |
32 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1121
|
source |
: AC6
|
|
25)
|
chain |
I |
residue |
75 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
26)
|
chain |
I |
residue |
78 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
27)
|
chain |
I |
residue |
103 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
28)
|
chain |
I |
residue |
106 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN I 1122
|
source |
: AC7
|
|
29)
|
chain |
J |
residue |
7 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
30)
|
chain |
J |
residue |
10 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
31)
|
chain |
J |
residue |
45 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
32)
|
chain |
J |
residue |
46 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN J 1066
|
source |
: AC8
|
|
33)
|
chain |
L |
residue |
31 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
34)
|
chain |
L |
residue |
34 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
35)
|
chain |
L |
residue |
48 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
36)
|
chain |
L |
residue |
51 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN L 1071
|
source |
: AC9
|
|
37)
|
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
|
|
38)
|
chain |
I |
residue |
7 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
39)
|
chain |
I |
residue |
10 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
40)
|
chain |
I |
residue |
29 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
41)
|
chain |
I |
residue |
32 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
42)
|
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
|
|
43)
|
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
|
|
44)
|
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
|
|
45)
|
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
|
|
46)
|
chain |
I |
residue |
40 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:18407956
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
47)
|
chain |
B |
residue |
977-989 |
type |
prosite |
sequence |
GDKFASRHGQKGT
|
description |
RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
|
source |
prosite : PS01166
|
|
48)
|
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
|
|
49)
|
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
|
|
50)
|
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
|
|
51)
|
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
|
|
52)
|
chain |
I |
residue |
75-110 |
type |
prosite |
sequence |
CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
|
description |
ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
|
source |
prosite : PS00466
|
|
53)
|
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
|
|
54)
|
chain |
B |
residue |
837 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
55)
|
chain |
A |
residue |
483 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
56)
|
chain |
A |
residue |
485 |
type |
catalytic |
sequence |
D
|
description |
788
|
source |
MCSA : MCSA1
|
|
57)
|
chain |
A |
residue |
483 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
58)
|
chain |
A |
residue |
485 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
59)
|
chain |
A |
residue |
107 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
60)
|
chain |
A |
residue |
110 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
61)
|
chain |
A |
residue |
148 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
62)
|
chain |
A |
residue |
167 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
63)
|
chain |
A |
residue |
481 |
type |
ZN_FING |
sequence |
D
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
64)
|
chain |
L |
residue |
31-51 |
type |
ZN_FING |
sequence |
CAECSSKLSLSRTDAVRCKDC
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
65)
|
chain |
J |
residue |
10 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
66)
|
chain |
J |
residue |
45 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
67)
|
chain |
J |
residue |
46 |
type |
ZN_FING |
sequence |
C
|
description |
C4-type
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
68)
|
chain |
B |
residue |
1185 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
69)
|
chain |
L |
residue |
31 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
70)
|
chain |
L |
residue |
34 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
71)
|
chain |
L |
residue |
48 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
72)
|
chain |
L |
residue |
51 |
type |
BINDING |
sequence |
C
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|