2I2R
Crystal structure of the KChIP1/Kv4.3 T1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005249 | molecular_function | voltage-gated potassium channel activity |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0008076 | cellular_component | voltage-gated potassium channel complex |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0005249 | molecular_function | voltage-gated potassium channel activity |
| B | 0006813 | biological_process | potassium ion transport |
| B | 0008076 | cellular_component | voltage-gated potassium channel complex |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0005249 | molecular_function | voltage-gated potassium channel activity |
| C | 0006813 | biological_process | potassium ion transport |
| C | 0008076 | cellular_component | voltage-gated potassium channel complex |
| C | 0051260 | biological_process | protein homooligomerization |
| D | 0005249 | molecular_function | voltage-gated potassium channel activity |
| D | 0006813 | biological_process | potassium ion transport |
| D | 0008076 | cellular_component | voltage-gated potassium channel complex |
| D | 0051260 | biological_process | protein homooligomerization |
| E | 0005509 | molecular_function | calcium ion binding |
| F | 0005509 | molecular_function | calcium ion binding |
| G | 0005509 | molecular_function | calcium ion binding |
| H | 0005509 | molecular_function | calcium ion binding |
| I | 0005249 | molecular_function | voltage-gated potassium channel activity |
| I | 0006813 | biological_process | potassium ion transport |
| I | 0008076 | cellular_component | voltage-gated potassium channel complex |
| I | 0051260 | biological_process | protein homooligomerization |
| J | 0005249 | molecular_function | voltage-gated potassium channel activity |
| J | 0006813 | biological_process | potassium ion transport |
| J | 0008076 | cellular_component | voltage-gated potassium channel complex |
| J | 0051260 | biological_process | protein homooligomerization |
| K | 0005249 | molecular_function | voltage-gated potassium channel activity |
| K | 0006813 | biological_process | potassium ion transport |
| K | 0008076 | cellular_component | voltage-gated potassium channel complex |
| K | 0051260 | biological_process | protein homooligomerization |
| L | 0005249 | molecular_function | voltage-gated potassium channel activity |
| L | 0006813 | biological_process | potassium ion transport |
| L | 0008076 | cellular_component | voltage-gated potassium channel complex |
| L | 0051260 | biological_process | protein homooligomerization |
| M | 0005509 | molecular_function | calcium ion binding |
| N | 0005509 | molecular_function | calcium ion binding |
| O | 0005509 | molecular_function | calcium ion binding |
| P | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 501 |
| Chain | Residue |
| F | ASP135 |
| F | ASN137 |
| F | ASP139 |
| F | TYR141 |
| F | GLU146 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 502 |
| Chain | Residue |
| H | GLU146 |
| H | ASP135 |
| H | ASN137 |
| H | ASP139 |
| H | TYR141 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 503 |
| Chain | Residue |
| E | ASP135 |
| E | ASN137 |
| E | ASP139 |
| E | TYR141 |
| E | GLU146 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G 504 |
| Chain | Residue |
| G | ASP135 |
| G | ASN137 |
| G | ASP139 |
| G | TYR141 |
| G | GLU146 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA P 505 |
| Chain | Residue |
| P | ASP135 |
| P | ASN137 |
| P | ASP139 |
| P | TYR141 |
| P | GLU146 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA M 506 |
| Chain | Residue |
| M | ASP135 |
| M | ASN137 |
| M | ASP139 |
| M | TYR141 |
| M | GLU146 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA N 507 |
| Chain | Residue |
| N | ASP135 |
| N | ASN137 |
| N | ASP139 |
| N | TYR141 |
| N | GLU146 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA O 508 |
| Chain | Residue |
| O | ASP135 |
| O | ASN137 |
| O | ASP139 |
| O | TYR141 |
| O | GLU146 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 509 |
| Chain | Residue |
| F | ASP183 |
| F | ASN185 |
| F | ASP187 |
| F | ILE189 |
| F | GLU194 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 510 |
| Chain | Residue |
| H | ASP183 |
| H | ASN185 |
| H | ASP187 |
| H | ILE189 |
| H | GLU194 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 511 |
| Chain | Residue |
| E | ASP183 |
| E | ASN185 |
| E | ASP187 |
| E | ILE189 |
| E | GLU194 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA G 512 |
| Chain | Residue |
| G | ASP183 |
| G | ASN185 |
| G | ASP187 |
| G | ILE189 |
| G | GLU194 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA P 513 |
| Chain | Residue |
| P | ASP183 |
| P | ASN185 |
| P | ASP187 |
| P | ILE189 |
| P | GLU194 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA M 514 |
| Chain | Residue |
| M | ASP183 |
| M | ASN185 |
| M | ASP187 |
| M | ILE189 |
| M | GLU194 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA N 515 |
| Chain | Residue |
| N | ASP183 |
| N | ASN185 |
| N | ASP187 |
| N | ILE189 |
| N | GLU194 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA O 516 |
| Chain | Residue |
| O | ASP183 |
| O | ASN185 |
| O | ASP187 |
| O | ILE189 |
| O | GLU194 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 601 |
| Chain | Residue |
| A | HIS104 |
| A | CYS131 |
| A | CYS132 |
| B | CYS110 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | HIS104 |
| B | CYS131 |
| B | CYS132 |
| C | CYS110 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 603 |
| Chain | Residue |
| C | HIS104 |
| C | CYS131 |
| C | CYS132 |
| D | CYS110 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 604 |
| Chain | Residue |
| A | CYS110 |
| D | HIS104 |
| D | CYS131 |
| D | CYS132 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN I 605 |
| Chain | Residue |
| J | CYS110 |
| I | HIS104 |
| I | CYS131 |
| I | CYS132 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN J 606 |
| Chain | Residue |
| J | HIS104 |
| J | CYS131 |
| J | CYS132 |
| K | CYS110 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN K 607 |
| Chain | Residue |
| K | HIS104 |
| K | CYS131 |
| K | CYS132 |
| L | CYS110 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN L 608 |
| Chain | Residue |
| I | CYS110 |
| L | HIS104 |
| L | CYS131 |
| L | CYS132 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA H 701 |
| Chain | Residue |
| H | GLU43 |
| H | THR46 |
| H | PHE48 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA F 702 |
| Chain | Residue |
| F | GLU43 |
| F | THR46 |
| F | PHE48 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA E 703 |
| Chain | Residue |
| E | GLU43 |
| E | THR46 |
| E | PHE48 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA G 704 |
| Chain | Residue |
| G | GLU43 |
| G | THR46 |
| G | PHE48 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DINKDGYINkeEM |
| Chain | Residue | Details |
| E | ASP135-MET147 | |
| E | ASP183-PHE195 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 109 |
| Details | Region: {"description":"Interaction with KCNIP1","evidences":[{"source":"UniProtKB","id":"Q9UK17","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"17057713","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2I2R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"in chain D","evidences":[{"source":"PubMed","id":"17057713","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2I2R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 280 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 280 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 280 |
| Details | Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 65 |
| Details | Region: {"description":"Interaction with KCND2","evidences":[{"source":"UniProtKB","id":"Q8R426","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17057713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17187064","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
