1g3b: Sequences

PDBeMotif: 1g3b

		Sequences				3D motifs				Ligand environment				Ligand bonds

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Enzyme:	3.4.21.4
Classification:	hydrolase \| release date: Mon, Oct 23, 2000
Title:	bovine beta-trypsin bound to meta-amidino schiff base magnesium(ii) chelate
Authors:	E.TOYOTA, H.SEKIZAKI, K.ITOH, K.K.S.NG, K.TANIZAWA, M.N.G.JAMES
Method:	X-RAY DIFFRACTION (resolution: 1.80Å)

PDBe Citation

Small molecules:

108

SO4

Ligand bond colours:

covalent

ionic

hydrogen

electrostatic

van-der-waals

plane-atom

plane-plane

undefined

- Click here to show 5Å bonds

Chain A sequence:
DDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPS
YNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQ
ITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

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 : BETA-TRYPSIN member of: CATH:2.40.10.10, GENE3D:G3DSA_2.40.10.10, PANTHER:PTHR24264, PFAM:PF00089, PRINTS:CHYMOTRYPSIN, PROSITE PATTERNS:PS00134/PS00135, PROSITE PROFILES:PS50240, SMART:SM00020, SUPERFAMILY:SSF50494, UniProt:P00760
`108` `601A`	`.. **** * * ** * *`
`SO4` `701A`	`.. ** \|\|\|\| \| \| \|\| \| \|`
`CA` `502A`	`.. * * * * \|\| \|\|\|\| \| \| \|\| \| \|`
`MG` `501A`	`.. \| \| \| \| \|\| \|\|\|\| \| \| \|\| \| \|`
`sec str:`	`......ee........eeeee...eeeeeeeee..eeeehhhhh....eeee............eeeeeeeeee.............eeeee........................eeeeee...............eeeeee..hhhhhhhhh.......eeee................eeee..eeeeeeee..........eeeee...hhhhhhhhhhh.`
`sequence :`	`..IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN`
`seq num:`	`..16 26 38 48 58 69 79 89 99 109 119 130 141 151 161 171 181 189 199 213 223 233`
`PKC_PHOSPHO_SITE`	`.. \| \| \| \| \| \| \|\|\|\| \|\| \|\|\|\|\| \| \| \| \| \|\| \|\|\|\| \| \|\| \| \| \| \| \|\|\| \| ^ \| \|\|\|\| \|\| \| \|\|\|\|\|\|\|\| \| \| ^ \| \| \| \| \| \| \|`
`CK2_PHOSPHO_SITE`	`.. \| \| \| \| \| \| \|\|\|\| \|\| \|\|\|\|\| \| \| \| \| \|\| \|\|\|\| \| \|\| \| \| \| ^***\| \| \| \| \|\|\|\| \|\| \| \|\|\|\|\|\|\|\| \| \| \| \| \| \| \| \| \|`
`MYRISTYL`	`.. ^*** \| \| \| ^*\|\| \|\| \|\|\|\|\| \| \| \| \| \|\| \|\|\|\| \| \|\| \| ^* \| \| \| \| \| ^*\| ^*\|\|\|\| \| \| ^*** \| \| \| \|`
`TRYPSIN_HIS`	`.. \| \| \| \| \|\| ***^\|\| \| \| \| \| \|\| \|\|\|\| \| \|\| \| \| \| \| \| \| \| \|\|\|\| \|\| \|\|\|\|\|\|\|\| \| \| \| \| \| \| \| \|`
`TRYPSIN_SER`	`.. \| \| \| \| \|\| \| \| \|\| \| \| \| \| \|\| \|\|\|\| \| \|\| \| \| \| \| \| \| \| \|\|\|\| \|\| \|****^*** \| \| \| \| \| \|`
`asxturn`	`.. \| \| \| *\| \| \| \|\| \| \| \| \| \|\|\|\| **\| \| \| \| \| \| \| \| \|\|\|\| \|\| \|\|\|\|\|\|\|\| \| \| \| \| \| \| \|`
`betaturn`	`.. \| \| \| \| \| \| \| \|\| \| \| \| \| \| \|\|\| \| \| \| \| \| \| \| \| **\|\| \|\| \|\|\|*** \| \| ** \| \|`
`nest`	`.. * \| \| \| \| \| \|\| \| \| \| \| \| * \| \| \| \| \| \| \| \| *\| \|\| \|\|\|\|\|* \| \| \| \| \|`
`niche`	`.. ** \| **** \|\|\| * * \| \| *** \|\|\|\|\|* ** \| \|`
`stmotif`	`.. \| \|\|\| ***** \| \| \|\|\|\|\|\| \| \|`
`ststaple`	`.. \| \|\|\| \| \| \|\|\|\|\|\| *****`
`stturn`	`.. \| * * \|\|\|\|\|\|`
`Catalytic site`	`.. * * ******`

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