eF-site ID 1n6p-A PDB Code 1n6p Chain A click to enlarge Title Crystal Structure of Human Rab5a A30E mutant complex with GppNHp Classification PROTEIN TRANSPORT Compound Ras-related protein Rab-5A Source Homo sapiens (Human) (RAB5A_HUMAN) Sequence A:  ICQFKLVLLGESEVGKSSLVLRFVKGQFHEFQESTIGAAF LTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAI VVYDITNEESFARAKNWVKELQRQASPNIVIALSGNKADL ANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAI AKKL Description Functional site 1) chain A residue 34 type sequence S description BINDING SITE FOR RESIDUE MG A 201 source : AC1 2) chain A residue 52 type sequence T description BINDING SITE FOR RESIDUE MG A 201 source : AC1 3) chain A residue 29 type sequence S description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 4) chain A residue 30 type sequence E description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 5) chain A residue 31 type sequence V description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 6) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 7) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 8) chain A residue 34 type sequence S description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 9) chain A residue 35 type sequence S description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 10) chain A residue 45 type sequence F description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 11) chain A residue 46 type sequence H description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 12) chain A residue 47 type sequence E description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 13) chain A residue 49 type sequence Q description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 14) chain A residue 51 type sequence S description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 15) chain A residue 52 type sequence T description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 16) chain A residue 78 type sequence G description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 17) chain A residue 133 type sequence N description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 18) chain A residue 134 type sequence K description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 19) chain A residue 136 type sequence D description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 20) chain A residue 137 type sequence L description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 21) chain A residue 163 type sequence S description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 22) chain A residue 164 type sequence A description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 23) chain A residue 165 type sequence K description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 24) chain A residue 180 type sequence K description BINDING SITE FOR RESIDUE GNP A 200 source : AC2 25) chain A residue 27 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12433916, ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H, ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N, ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P, ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q, ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH source Swiss-Prot : SWS_FT_FI1 26) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12433916, ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H, ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N, ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P, ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q, ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH source Swiss-Prot : SWS_FT_FI1 27) chain A residue 75 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12433916, ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H, ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N, ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P, ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q, ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH source Swiss-Prot : SWS_FT_FI1 28) chain A residue 133 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12433916, ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H, ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N, ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P, ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q, ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH source Swiss-Prot : SWS_FT_FI1 29) chain A residue 163 type BINDING sequence S description BINDING => ECO:0000269|PubMed:12433916, ECO:0000269|PubMed:14684892, ECO:0000269|PubMed:15378032, ECO:0000269|PubMed:20534488, ECO:0007744|PDB:1N6H, ECO:0007744|PDB:1N6L, ECO:0007744|PDB:1N6N, ECO:0007744|PDB:1N6O, ECO:0007744|PDB:1N6P, ECO:0007744|PDB:1N6R, ECO:0007744|PDB:1R2Q, ECO:0007744|PDB:1TU3, ECO:0007744|PDB:3MJH source Swiss-Prot : SWS_FT_FI1 30) chain A residue 84 type MOD_RES sequence S description Phosphoserine; by LRRK2 => ECO:0000269|PubMed:29125462 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 120 type CARBOHYD sequence R description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:32974215 source Swiss-Prot : SWS_FT_FI3

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