eF-site ID 5y7g-ABC PDB Code 5y7g Chain A, B, C click to enlarge Title Crystal structure of paFAN1 bound to 1nt 5'flap DNA with gap Classification HYDROLASE/DNA Compound Fanconi-associated nuclease 1 homolog Source Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (5Y7G) Sequence A:  ALPEPFYYLHNFRAVLAWIGERYADLLDDQERAFIAAFAE LPEASQALLVRMVMRKGTLFREGKLAYAEIGDTRAAVQPL LALGWVDAQPTLELAQLFGLLKKDELSQLFRDHLGRANLR KDALLERLQPLFPEARRLAEWQADFAEPVYELRCMALCDR LRLMYFGNLWQDWSEFVLADLGIYRYESVEFSADSRGFRL RADVDAYLHLFDCRQRFDLGEPLEELLAGLPGEPYANPWL EGRRVKLLFQFAQHCEKQRDFDLAQRLYRQSSHPGARLRA IRSLERGERFAEAHALAREASCAPESDAERQGLARLLPRL QGKLGLPRQARAAAPEIDRLDLCLAFPSEPCSVEWAVREH LEEPGCAVHYVENGLINSLFGLLCWEAIFAAIPGAFFHPF HSAPADLHSADFRQRRAALFEACLGRLEDGSYRDAIRCRY RDKFGLQSPFVYWELLGEELLEQALDCLPAAHLRAWFERL LEDIPGNRAGLPDLIQFWPAQRRYRMVEVKGPGDRLQDNQ LRWLQFCREREMPVAVCYVRWH B:  PEPFYYLHNFRAVLAWIGERYADLLDDQERAFIAAFAELP EASQALLVRMVMRKGTLFREGKLAYAEIGDTRAAVQPLLA LGWVDAQPTLELAQLFGLLKKDELSQLFRDHLGRANLRKD ALLERLQPLFPEARRLAEWQADFAEPVYELRCMALCDRLR LMYFGNLWQDWSEFVLADLGIYRYESVEFSADSRGFRLRA DVDAYLHLFDCRQRFDLGEPLEELLAGLPGEPYANPWLEG RRVKLLFQFAQHCEKQRDFDLAQRLYRQSSHPGARLRAIR SLERGERFAEAHALAREASCAPESDAERQGLARLLPRLQG KLGLPRQARAAAPEIDRLDLCLAFPSEPCSVEWAVREHLE EPGCAVHYVENGLINSLFGLLCWEAIFAAIPGAFFHPFHS APADLHSADFRQRRAALFEACLGRLEDGSYRDAIRCRYRD KFGLQSPFVYWELLGEELLEQALDCLPAAHLRAWFERLLE DIPGNRAGLPDLIQFWPAQRRYRMVEVKGPGDRLQDNQLR WLQFCREREMPVAVCYVRWHVDD C:  EPFYYLHNFRAVLAWIGERYADLLDDQERAFIAAFAELPE ASQALLVRMVMRKGTLFREGKLAYAEIGDTRAAVQPLLAL GWVDAQPTLELAQLFGLLKKDELSQLFRDHLGRANLRKDA LLERLQPLFPEARRLAEWQADFAEPVYELRCMALCDRLRL MYFGNLWQDWSEFVLADLGIYRYESVEFSADSRGFRLRAD VDAYLHLFDCRQRFDLGEPLEELLAGLPGEPYANPWLEGR RVKLLFQFAQHCEKQRDFDLAQRLYRQSSHPGARLRAIRS LERGERFAEAHALAREASCAPESDAERQGLARLLPRLQGK LGLPRQARAAAPEIDRLDLCLAFPSEPCSVEWAVREHLEE PGCAVHYVENGLINSLFGLLCWEAIFAAIPGAFFHPFHSA PADLHSADFRQRRAALFEACLGRLEDGSYRDAIRCRYRDK FGLQSPFVYWELLGEELLEQALDCLPAAHLRAWFERLLED IPGNRAGLPDLIQFWPAQRYRMVEVKGPGDRLQDNQLRWL QFCREREMPVAVCYVRWHVD Description Functional site 1) chain A residue 368 type sequence E description binding site for residue CA A 601 source : AC1 2) chain A residue 507 type sequence D description binding site for residue CA A 601 source : AC1 3) chain A residue 522 type sequence E description binding site for residue CA A 601 source : AC1 4) chain A residue 523 type sequence V description binding site for residue CA A 601 source : AC1 5) chain A residue 386 type sequence E description binding site for residue CA A 602 source : AC2 6) chain A residue 507 type sequence D description binding site for residue CA A 602 source : AC2 7) chain B residue 368 type sequence E description binding site for residue CA B 601 source : AC3 8) chain B residue 507 type sequence D description binding site for residue CA B 601 source : AC3 9) chain B residue 522 type sequence E description binding site for residue CA B 601 source : AC3 10) chain B residue 523 type sequence V description binding site for residue CA B 601 source : AC3 11) chain B residue 368 type sequence E description binding site for residue CA B 602 source : AC4 12) chain B residue 384 type sequence Y description binding site for residue CA B 602 source : AC4 13) chain B residue 386 type sequence E description binding site for residue CA B 602 source : AC4 14) chain B residue 507 type sequence D description binding site for residue CA B 602 source : AC4 15) chain C residue 368 type sequence E description binding site for residue CA C 601 source : AC5 16) chain C residue 507 type sequence D description binding site for residue CA C 601 source : AC5 17) chain C residue 522 type sequence E description binding site for residue CA C 601 source : AC5 18) chain C residue 523 type sequence V description binding site for residue CA C 601 source : AC5 19) chain C residue 524 type sequence K description binding site for residue CA C 601 source : AC5 20) chain A residue 386 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 21) chain C residue 507 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 22) chain C residue 522 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 523 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 507 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 522 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 523 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 386 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 507 type BINDING sequence D description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 522 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 523 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 386 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25319828, ECO:0007744|PDB:4R89 source Swiss-Prot : SWS_FT_FI1

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