eF-site ID 2jer-ABCDEFGH PDB Code 2jer Chain A, B, C, D, E, F, G, H click to enlarge Title Agmatine deiminase of Enterococcus faecalis catalyzing its reaction. Classification HYDROLASE Compound AGMATINE DEIMINASE Source (2JER) Sequence A:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRVG B:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKR C:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRVGG D:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRVGGKQNSS E:  MAKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRD GGKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPP EITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWG GLVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGS FHVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNV EKVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQN SPFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIK GSFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYG DENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQ QEPKRVGG F:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRVGG G:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRVG H:  AKRIVGSTPKQDGFRMPGEFEPQEKVWMIWPERPDNWRDG GKPVQEAFTNVAKAISQFTPMNVVVSQQQFQNCRRQLPPE ITVYEMSNNDAWVRDCGPSFVINDHGEIRGVDWTFNAWGG LVDGLYFPWDQDDLVAQKICEIEHVDSYRTDDFVLEGGSF HVDGQGTVLTTEMCLLSEGRNPQLSKEAIEQKLCDYLNVE KVLWLGDGIDPEETNGHVDDVACFIAPGEVACIYTEDQNS PFYEAAQDAYQRLLKMTDAKGRQLKVHKLCCPVKNVTIKG SFKIDFVEGTMPREDGDICIASYMNFLITNDGVIVPQYGD ENDRLALEQVQTMFPDKKIVGVNTVEVVYGGGNIHXITQQ EPKRV Description Functional site 1) chain A residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 2) chain B residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 3) chain C residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 4) chain D residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 5) chain E residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 6) chain F residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 7) chain G residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 8) chain H residue 357 type ACT_SITE sequence X description Amidino-cysteine intermediate => ECO:0000255|HAMAP-Rule:MF_01841, ECO:0000269|PubMed:17028272, ECO:0007744|PDB:2JER source Swiss-Prot : SWS_FT_FI1 9) chain A residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 10) chain E residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 11) chain F residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 12) chain F residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 13) chain G residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 14) chain G residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 15) chain H residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 16) chain H residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 22) chain D residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 23) chain D residue 220 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2 24) chain E residue 214 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:G7JT50 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links