eF-site ID 3cmm-A
PDB Code 3cmm
Chain A

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Title Crystal Structure of the Uba1-Ubiquitin Complex
Classification LIGASE/PROTEIN BINDING
Compound Ubiquitin-activating enzyme E1 1
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (UBIQ_YEAST)
Sequence A:  GEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEI
AKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKR
GDVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDT
VSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDEF
TVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGNFV
RFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYKK
GGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQ
LHLGFQALHQFAVRHNGELPRTMNDEDANELIKLVTDLSV
QQPEVLGEGVDVNEDLIKELSYQARGDIPGVVAFFGGLVA
QEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTTQ
PVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLK
NWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVG
KNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFNDS
FWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGT
KGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKIDH
TIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKDVKGV
LESISDSLSSKPHNFEDCIKWARLEFEKKFNHDIKQLLFN
FPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAG
ASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEFTPNA
NLKIQVNDDDPDPEIDQLVSSLPDPSTLAGFKLEPVDFEK
DDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIAGRII
PAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVNLAL
PFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLI
EHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERLNLPIT
QLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFITIH
L
Description


Functional site

1) chain A
residue 316
type
sequence D
description BINDING SITE FOR RESIDUE PRO A 5119
source : AC1

2) chain A
residue 320
type
sequence N
description BINDING SITE FOR RESIDUE PRO A 5119
source : AC1

3) chain A
residue 21
type catalytic
sequence R
description 307
source MCSA : MCSA1

4) chain A
residue 481
type catalytic
sequence R
description 307
source MCSA : MCSA1

5) chain A
residue 544
type catalytic
sequence D
description 307
source MCSA : MCSA1

6) chain A
residue 600
type catalytic
sequence C
description 307
source MCSA : MCSA1

7) chain A
residue 601
type catalytic
sequence T
description 307
source MCSA : MCSA1

8) chain A
residue 603
type catalytic
sequence R
description 307
source MCSA : MCSA1

9) chain A
residue 781
type catalytic
sequence N
description 307
source MCSA : MCSA1

10) chain A
residue 782
type catalytic
sequence D
description 307
source MCSA : MCSA1

11) chain A
residue 600
type catalytic
sequence C
description 939
source MCSA : MCSA2

12) chain A
residue 601
type catalytic
sequence T
description 939
source MCSA : MCSA2

13) chain A
residue 603
type catalytic
sequence R
description 939
source MCSA : MCSA2

14) chain A
residue 781
type catalytic
sequence N
description 939
source MCSA : MCSA2

15) chain A
residue 782
type catalytic
sequence D
description 939
source MCSA : MCSA2

16) chain A
residue 914
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI4

17) chain A
residue 595
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI5

18) chain A
residue 608
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
source Swiss-Prot : SWS_FT_FI5

19) chain A
residue 376-384
type prosite
sequence KACSGKFTP
description UBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFtP
source prosite : PS00536

20) chain A
residue 598-606
type prosite
sequence PLCTLRSFP
description UBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PLCTLRsFP
source prosite : PS00865

21) chain A
residue 444
type CROSSLNK
sequence A
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 481
type CROSSLNK
sequence R
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 544
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
source Swiss-Prot : SWS_FT_FI2


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