eF-site ID 3puf-ABCDEFGHIJKLMNOPQR
PDB Code 3puf
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R

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Title Crystal structure of human RNase H2 complex
Classification HYDROLASE
Compound Ribonuclease H2 subunit A
Source null (RNH2C_HUMAN)
Sequence A:  MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGP
VLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLF
AKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDT
ATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGI
EVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQ
TDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQT
ILEKEAEDVIWEDSSHRYFLERGLESATSL
B:  MRQHVFLVSEYLLMFVKLVNPCSGEGAIYLFNMCLQQLFE
VKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLI
KADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVT
EEKGNPKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNEE
DYIRYAHGLISDYIPKELSDDLSKY
C:  AIERHRVHLRSATLRDAVPATLHLLPCEVAVDGPAPVGRF
FTPAIRQGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTE
EDRFIGATANFSRFTLWGLETIPGPDAKVRGALTWPSLAA
AIHAQVP
D:  DLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPV
LGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFA
KMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTA
TGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIE
VTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQD
LDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTA
QTILEKEAEDVIWEDSASSHRYFLERGLESATSL
E:  MRQHVFLVSEYLKDMKNGLMFVKLVNPCSGEGAIYLFNMC
LQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFL
LLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEK
LLHHVTKYYKYSKEKTLKWLEKKVNQTVAALKTNNVKEED
YIRYAHGLISDYIPKELSDDL
F:  AIERHRVHLRSATLRDAVPATLHLLPCEVAVDGPAPVGRF
FTPAIRQGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTE
EFDRFIGATANFSRFTLWGLETIPGPDAKVRGALTWPSLA
AAIHAQVP
G:  DNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYA
ICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDF
VGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYA
LDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKA
DALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGS
GYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKE
AEDVIWEDSASHRYFLERGLESATSL
H:  HMRQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGEGAIY
LFNMCLQQLFEVKVFKEKHHSWFINQSVQSGGLLHFATPV
DPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKL
PGLEKLLHHVTEEKGNKKYYKYSKEKTLKWLEKKVNQTVA
ALKTNNVNVSSRVKEEDYIRYAHGLISDYIPKELSDDLSK
YL
I:  AAIERHRVHLRSATLRAVPATLHLLPCEVAVDGPAPVGRF
FTPAIRQGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTE
EKKVSEEEPLERDFDRFIGATANFSRFTLWGLETIPGPDA
KVRGALTWPSLAAAIHAQVP
J:  LSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVL
GPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAK
MEDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGL
IQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTV
KAKADALYPVVSAASICAKVARDQAVKKWQFVEKLDLDTD
YGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTIL
EKEAEDVIWEDSASSHRYFLERGLESATSL
K:  HMRQHVFLVSEYLLMFVKLVNPCSGEGAIYLFNMCLQQLF
EVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYL
IKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHV
TEEKKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNDYIR
YAHGLISDYIPKELSDDLSKYL
L:  ERHRVHLRRDAVPATLHLLPCEVAVDGPAPVGRFFTPAIR
QGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEIGATAN
FSRFTLWGLETIPGPDAKVRGALTWPSLAAAIHAQV
M:  DLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPV
LGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFA
KMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTA
TGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIE
VTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQD
LDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTA
QTILEKEAEDVIWEDSSHRYFLERGLESATSL
N:  MRQHVFLVSEYLKLMFVKLVNPCSGEGAIYLFNMCLQQLF
EVKVFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYL
IKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHV
TEEKDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVS
SEDYIRYAHGLISDYIPKELSDDLSK
O:  IERHRVHLVPATLHLLPCEVAVDGPAPVGRFFTPAIRQGP
EGLEVSFRGRCLRGEEVAVPPGLVGYVMVTRFIGATANFS
RFTLWGLETIPGPDAKVRGALTWPSLAAAIHAQVPE
P:  ELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGP
MVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKME
DTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGL
IQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTV
KAKADALYPVVSAASICAKVARDQAVKKWQFVEGSGYPND
PKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVI
WEDSHRYFLERGLESATSL
Q:  MRQHVFLVSELMFVKLVNPCSGEGAIYLFNMCLQQLFEVK
VFKEKHHSWFINQSVQSGGLLHFATPVDPLFLLLHYLIKA
DKEKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEK
KYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVIRYAHGLI
SDYIPKELSDDLSKYL
R:  ERHRVHLRVPATLHLLPCEVAVDGPAPVGRFFTPAIRQGP
EGLEVSFRGRCLRGEEVAVPPGLVGYVMVTDRFIGATANF
SRFTLWGLETIPGPDAKVRGALTWPSLAAAIHAQV
Description


Functional site

1) chain G
residue 34
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

2) chain G
residue 35
type MOD_RES
sequence E
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

3) chain G
residue 141
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

4) chain J
residue 34
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

5) chain J
residue 35
type MOD_RES
sequence E
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

6) chain J
residue 141
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

7) chain M
residue 34
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

8) chain M
residue 35
type MOD_RES
sequence E
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

9) chain M
residue 141
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

10) chain P
residue 34
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

11) chain P
residue 35
type MOD_RES
sequence E
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

12) chain P
residue 141
type MOD_RES
sequence D
description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 204
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

14) chain A
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

15) chain D
residue 204
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

16) chain D
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

17) chain G
residue 204
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

18) chain G
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

19) chain J
residue 204
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

20) chain J
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

21) chain M
residue 204
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

22) chain M
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

23) chain P
residue 216
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:18669648
source Swiss-Prot : SWS_FT_FI3

24) chain A
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4

25) chain D
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4

26) chain G
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4

27) chain J
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4

28) chain M
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4

29) chain P
residue 257
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CWY8
source Swiss-Prot : SWS_FT_FI4


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