eF-site ID 2a78-AB PDB Code 2a78 Chain A, B click to enlarge Title Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme Classification PROTEIN BINDING/TRANSFERASE Compound Ras-related protein Ral-A Source Homo sapiens (Human) (ARC3_CBDP) Sequence A:  ALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYR KKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCV FSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLE DKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLM REIRARKMED B:  TYQEFTNIDQAKAWGNAQYKKYGLSKSEKEAIVSYTKSAS EINGKLRQNKGVINGFPSNLIKQVELLDKSFNKMKTPENI MLFRGDDPAYLGTEFQNTLLNSNGTINKTAFEKAKAKFLN KDRLEYGYISTSLMNVSQFAGRPIITKFKVAKGSKAGYID PISAFAGQLEMLLPRHSTYHIDDMRLSSDGKQIIITATMM GTAINPK Description Functional site 1) chain A residue 28 type sequence S description BINDING SITE FOR RESIDUE MG A 400 source : AC1 2) chain A residue 24 type sequence G description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 3) chain A residue 25 type sequence V description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 4) chain A residue 26 type sequence G description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 5) chain A residue 27 type sequence K description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 6) chain A residue 28 type sequence S description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 7) chain A residue 29 type sequence A description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 8) chain A residue 41 type sequence E description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 9) chain A residue 42 type sequence D description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 10) chain A residue 127 type sequence N description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 11) chain A residue 128 type sequence K description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 12) chain A residue 130 type sequence D description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 13) chain A residue 131 type sequence L description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 14) chain A residue 157 type sequence S description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 15) chain A residue 158 type sequence A description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 16) chain A residue 159 type sequence K description BINDING SITE FOR RESIDUE GDP A 500 source : AC2 17) chain B residue 174 type catalytic sequence S description 824 source MCSA : MCSA1 18) chain B residue 214 type catalytic sequence E description 824 source MCSA : MCSA1 19) chain B residue 128 type ACT_SITE sequence R description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 174 type ACT_SITE sequence S description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 214 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01340 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 80 type BINDING sequence T description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 91 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 128 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 26) chain B residue 167 type BINDING sequence R description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 183 type BINDING sequence F description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 212 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:16177825 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 214 type SITE sequence E description Transition state stabilizer source Swiss-Prot : SWS_FT_FI3

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