3eug: Sequences

PDBeMotif: 3eug

		Sequences				3D motifs				Ligand environment				Ligand bonds

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Enzyme:	3.2.2.3
Classification:	hydrolase \| release date: Tue, Oct 13, 1998
Title:	crystal structure of escherichia coli uracil dna glycosylase complexes with uracil and glycerol: structure and glycosyla mechanism revisited
Authors:	A.C.DROHAT, G.L.GILL, G.XIAO, J.JAGADEESH, J.T.STIVERS, M.TORDOVA
Method:	X-RAY DIFFRACTION (resolution: 1.43Å)

PDBe Citation

Small molecules:

GOL

Ligand bond colours:

covalent

ionic

hydrogen

electrostatic

van-der-waals

plane-atom

plane-plane

undefined

- Click here to show 5Å bonds

Chain A sequence:
MANELTWHDVLAEEKQQPHFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVR
PGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVV
FLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQHGETPIDWMPVLPAESE

Residue colours: hydrophilic hydrophobic intermediate

Assembly 1

View the assembly/model: (

)

Motif search

chain:

Sequence numbers:

Using:	φ/ψ residues code secondary structures
	coordinates of: Cαs Side-chain

View the fragment:

chain A : PROTEIN (GLYCOSYLASE) member of: CATH:3.40.470.10, GENE3D:G3DSA_3.40.470.10, HAMAP:MF_00148, PANTHER:PTHR11264/PTHR11264_SF4, PFAM:PF03167, PROSITE PATTERNS:PS00130, SMART:SM00986/SM00987, SUPERFAMILY:SSF52141, TIGRFAMS:TIGR00628, UniProt:P12295
`GOL` `231A`	`.. * * * * *`
`GOL` `230A`	`.. \| \| \| \| \| ** * ** * *`
`sec str:`	`....hhhhh..hhh.hhhhhhhhhhhhhhhh.......hhh..hhhhh..hhh..eeeee........................hhhhhhhhhhh..............hhhhhh.eeeee.................hhhhhhhhhhhhhhh....eeeee.hhhhhh.........eeeee.......hhh......hhhhhhhhhhh.................`
`sequence :`	`..LTWHDVLAEEKQQPHFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQHGETPIDWMPVLPAESE`
`seq num:`	`..5 15 25 35 45 55 65 75 85 95 105 115 125 135 145 155 165 175 185 195 205 215 225`
`PKC_PHOSPHO_SITE`	`.. \| \| \|\| \|\| \|\|\| \| ^ \| \| \| \| \| \|\|\| \|\|\| \| \| \| \| \| \| ^ \| \|\|\| \|\| \| \| \| \| \| \| ^ \|\| \|\|\|\| \| ^ \| \| \| \| \|\| \|\|\|\| \| \| \| \|\|\| \|\|\|\|\|\|\|\|\| \| \|\|\|\| \| \|`
`CK2_PHOSPHO_SITE`	`.. ^* \|\| \|\| \|\|\| \| \| \| \| \| \| \| \|\|\| \|\|\| \| \| \| \| \| \| \| \| \| \|\|\| \|\| \| \| \| \| \| \| \| \|\| \|\|\|\| ^* \| \| \| \| \|\| \|\|\|\| \| \| \| \|\|\| \|\|\|\|\|\|\|\|\| \| \|\|\|^*** \|`
`MYRISTYL`	`.. \|\| \|\| \|\|\| \| \| \| \| \| \| \| \|\|\| \|\|\| \| \| \| ^*** \| \| \| \|\|\| \|\| \| \| \| \| \| \| \| ^***\| \| \| \| \| \|\| \|\|\|\| \| \| \| \|\|\| \|\|\|\|\|\|\|\|\| \| \|\|\| \| \|`
`U_DNA_GLYCOSYLASE`	`.. \|\| \|\| \|\|\| \| \| \| \| \| \| \| \|\|\| \|\|*****^ \| \| \| \| \| \| \| \|\|\| \|\| \| \| \| \| \| \| \| \| \|\|\|\| \| \| \| \| \|\| \|\|\|\| \| \| \| \|\|\| \|\|\|\|\|\|\|\|\| \| \|\|\| \| \|`
`alphabetamotif`	`.. \|\| \|*** \| \| \| \| \| \| \| \|* \| \| \| \| \| \| \| \| \| \|* \| \| \| \| \| \| \| \| \|\|\|\| \| \| \| \| \|\| \|\|\|\| \| \| *** \|\|\|\|\|\|\|\|\| \| \|\|\| \| \|`
`asxturn`	`.. \|\| \|\| \|\| \| \| \| \| \| \| \| \|\|\| \|\| \| \| \| \| \| \| \| \| \| \|\|\| \|\| \| \| \| \| \| \| \| \| \|\|\|\| \| \| \| \| \|\| \|*** \| \| \| \|\|\| \|\|\|\|\|\|\|\|\| \| \|\|\| \| \|`
`betaturn`	`.. ****** \| \| \| \|\| \| \| \| \| \| \| \| \|**** \| \| \| ***** \| \| \| \| \| \| \| ***\|\|\|\|\|\|\|\| **\| \| \|`
`nest`	`.. \| \| \| \| * \| \| \| \| \| \| \| * \| \| \| \| \| \| \|\| \| \| \| * * \| \| \| \| \| \| \| \| \| \|\|\| ******* * \| \|`
`niche`	`.. ** \| \| \| * ** \| *** * ***** * \|\|\| ***`
`stmotif`	`.. \| \| \| \| \| \| *****`
`ststaple`	`.. *** \| * ****`
`stturn`	`.. \| \| ***`
`Catalytic site`	`.. * *`

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