eF-site ID 5bsh-ABCDEFGHIJ PDB Code 5bsh Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Crystal structure of Medicago truncatula (delta)1-Pyrroline-5-Carboxylate Reductase (MtP5CR) in complex with L-Proline Classification OXIDOREDUCTASE Compound Pyrroline-5-carboxylate reductase Source Medicago truncatula (Barrel medic) (Medicago tribuloides) (G7KRM5_MEDTR) Sequence A:  IIPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKT AIHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQ LLKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERF IRVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIG KIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGL PRDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGT TIAGVHELEKAGFRGILMNAVVAAAKRSQELS B:  IIPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKT AIHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQ LLKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERF IRVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIG KIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGL PRDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGT TIAGVHELEKAGFRGILMNAVVAAAKRSQELS C:  PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAS NPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQLLKD VVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERFIRVM PNTAATVGEAASVMSLGGAATEEDANLISQLFGSIGKIWK ADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPRDL ALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAG VHELEKAGFRGILMNAVVAAAKRSQELS D:  PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAS NPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQLLKD VVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERFIRVM PNTAATVGEAASVMSLGGAATEEDANLISQLFGSIGKIWK ADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPRDL ALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAG VHELEKAGFRGILMNAVVAAAKRSQELS E:  IIPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKT AIHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQ LLKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERF IRVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIG KIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGL PRDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGT TIAGVHELEKAGFRGILMNAVVAAAKRSQELS F:  IIPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKT AIHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQ LLKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERF IRVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIG KIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGL PRDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGT TIAGVHELEKAGFRGILMNAVVAAAKRSQELS G:  PADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAARR TAFESIGITVLSSNDDVVRDSNVVVFSVKPQLLKDVVLKL KPLLTKDKLLVSVAAGIKMKDLQEWAGHERFIRVMPNTAA TVGEAASVMSLGGAATEEDANLISQLFGSIGKIWKADDKY FDAITGLSGSGPAYIYLAIEALADGGVAAGLPRDLALSLA SQTVLGAASMATQSGKHPGQLKDDVTSPGGTTIAGVHELE KAGFRGILMNAVVAAAKRSQELS H:  IIPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKT AIHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQ LLKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERF IRVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIG KIWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGL PRDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGT TIAGVHELEKAGFRGILMNAVVAAAKRSQELS I:  PIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTAI HSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQLL KDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERFIR VMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIGKI WKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLPR DLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTTI AGVHELEKAGFRGILMNAVVAAAKRSQELS J:  IPIPADSYTLGFIGAGKMAESIAKGAVRSGVLSPSRIKTA IHSNPARRTAFESIGITVLSSNDDVVRDSNVVVFSVKPQL LKDVVLKLKPLLTKDKLLVSVAAGIKMKDLQEWAGHERFI RVMPNTAATVGEAASVMSLGGAATEEDANLISQLFGSIGK IWKADDKYFDAITGLSGSGPAYIYLAIEALADGGVAAGLP RDLALSLASQTVLGAASMATQSGKHPGQLKDDVTSPGGTT IAGVHELEKAGFRGILMNAVVAAAKRSQELS Description Functional site 1) chain A residue 236 type sequence V description binding site for residue PRO A 301 source : AC1 2) chain A residue 238 type sequence S description binding site for residue PRO A 301 source : AC1 3) chain A residue 241 type sequence G description binding site for residue PRO A 301 source : AC1 4) chain A residue 242 type sequence T description binding site for residue PRO A 301 source : AC1 5) chain A residue 243 type sequence T description binding site for residue PRO A 301 source : AC1 6) chain B residue 180 type sequence G description binding site for residue PRO A 301 source : AC1 7) chain A residue 180 type sequence G description binding site for residue PRO B 301 source : AC2 8) chain B residue 236 type sequence V description binding site for residue PRO B 301 source : AC2 9) chain B residue 238 type sequence S description binding site for residue PRO B 301 source : AC2 10) chain B residue 241 type sequence G description binding site for residue PRO B 301 source : AC2 11) chain B residue 242 type sequence T description binding site for residue PRO B 301 source : AC2 12) chain B residue 243 type sequence T description binding site for residue PRO B 301 source : AC2 13) chain C residue 236 type sequence V description binding site for residue PRO C 301 source : AC3 14) chain C residue 238 type sequence S description binding site for residue PRO C 301 source : AC3 15) chain C residue 241 type sequence G description binding site for residue PRO C 301 source : AC3 16) chain C residue 242 type sequence T description binding site for residue PRO C 301 source : AC3 17) chain C residue 243 type sequence T description binding site for residue PRO C 301 source : AC3 18) chain D residue 180 type sequence G description binding site for residue PRO C 301 source : AC3 19) chain C residue 180 type sequence G description binding site for residue PRO D 301 source : AC4 20) chain D residue 236 type sequence V description binding site for residue PRO D 301 source : AC4 21) chain D residue 238 type sequence S description binding site for residue PRO D 301 source : AC4 22) chain D residue 241 type sequence G description binding site for residue PRO D 301 source : AC4 23) chain D residue 242 type sequence T description binding site for residue PRO D 301 source : AC4 24) chain D residue 243 type sequence T description binding site for residue PRO D 301 source : AC4 25) chain E residue 236 type sequence V description binding site for residue PRO E 301 source : AC5 26) chain E residue 238 type sequence S description binding site for residue PRO E 301 source : AC5 27) chain E residue 241 type sequence G description binding site for residue PRO E 301 source : AC5 28) chain E residue 242 type sequence T description binding site for residue PRO E 301 source : AC5 29) chain E residue 243 type sequence T description binding site for residue PRO E 301 source : AC5 30) chain F residue 180 type sequence G description binding site for residue PRO E 301 source : AC5 31) chain E residue 180 type sequence G description binding site for residue PRO F 301 source : AC6 32) chain F residue 236 type sequence V description binding site for residue PRO F 301 source : AC6 33) chain F residue 238 type sequence S description binding site for residue PRO F 301 source : AC6 34) chain F residue 241 type sequence G description binding site for residue PRO F 301 source : AC6 35) chain F residue 242 type sequence T description binding site for residue PRO F 301 source : AC6 36) chain F residue 243 type sequence T description binding site for residue PRO F 301 source : AC6 37) chain G residue 236 type sequence V description binding site for residue PRO G 301 source : AC7 38) chain G residue 238 type sequence S description binding site for residue PRO G 301 source : AC7 39) chain G residue 241 type sequence G description binding site for residue PRO G 301 source : AC7 40) chain G residue 242 type sequence T description binding site for residue PRO G 301 source : AC7 41) chain G residue 243 type sequence T description binding site for residue PRO G 301 source : AC7 42) chain H residue 176 type sequence T description binding site for residue PRO G 301 source : AC7 43) chain H residue 180 type sequence G description binding site for residue PRO G 301 source : AC7 44) chain G residue 180 type sequence G description binding site for residue PRO H 301 source : AC8 45) chain H residue 236 type sequence V description binding site for residue PRO H 301 source : AC8 46) chain H residue 238 type sequence S description binding site for residue PRO H 301 source : AC8 47) chain H residue 241 type sequence G description binding site for residue PRO H 301 source : AC8 48) chain H residue 242 type sequence T description binding site for residue PRO H 301 source : AC8 49) chain H residue 243 type sequence T description binding site for residue PRO H 301 source : AC8 50) chain I residue 236 type sequence V description binding site for residue PRO I 301 source : AC9 51) chain I residue 238 type sequence S description binding site for residue PRO I 301 source : AC9 52) chain I residue 241 type sequence G description binding site for residue PRO I 301 source : AC9 53) chain I residue 242 type sequence T description binding site for residue PRO I 301 source : AC9 54) chain I residue 243 type sequence T description binding site for residue PRO I 301 source : AC9 55) chain J residue 180 type sequence G description binding site for residue PRO I 301 source : AC9 56) chain I residue 180 type sequence G description binding site for residue PRO J 301 source : AD1 57) chain J residue 236 type sequence V description binding site for residue PRO J 301 source : AD1 58) chain J residue 238 type sequence S description binding site for residue PRO J 301 source : AD1 59) chain J residue 241 type sequence G description binding site for residue PRO J 301 source : AD1 60) chain J residue 242 type sequence T description binding site for residue PRO J 301 source : AD1 61) chain J residue 243 type sequence T description binding site for residue PRO J 301 source : AD1 62) chain A residue 229-251 type prosite sequence PGQLKDDVTSPGGTTIAGVHELE description P5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkddVTSpGGtTiaGVheLE source prosite : PS00521

Display surface Download Links