1F3M
CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 601 |
| Chain | Residue |
| A | ASN132 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD C 602 |
| Chain | Residue |
| C | ASN468 |
| C | LEU470 |
| C | IOD616 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 603 |
| Chain | Residue |
| D | HOH631 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD D 604 |
| Chain | Residue |
| D | PRO325 |
| D | IOD628 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 605 |
| Chain | Residue |
| C | HOH653 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 607 |
| Chain | Residue |
| A | LYS114 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD B 608 |
| Chain | Residue |
| A | GLN102 |
| A | HOH667 |
| B | GLY98 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 609 |
| Chain | Residue |
| C | HOH628 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD C 610 |
| Chain | Residue |
| C | ASN466 |
| D | LYS268 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 611 |
| Chain | Residue |
| C | GLY364 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 613 |
| Chain | Residue |
| C | PRO325 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD A 614 |
| Chain | Residue |
| A | LYS119 |
| B | IOD615 |
| B | HOH652 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IOD B 615 |
| Chain | Residue |
| A | ASN120 |
| A | IOD614 |
| B | LYS119 |
| C | HOH695 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD C 616 |
| Chain | Residue |
| A | HOH640 |
| C | IOD602 |
| C | HOH629 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 617 |
| Chain | Residue |
| B | HOH660 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 619 |
| Chain | Residue |
| D | MET399 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 620 |
| Chain | Residue |
| A | LYS134 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 621 |
| Chain | Residue |
| D | GLY364 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD D 622 |
| Chain | Residue |
| D | ASP265 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD C 623 |
| Chain | Residue |
| C | LYS444 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD B 624 |
| Chain | Residue |
| B | HOH631 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD D 625 |
| Chain | Residue |
| C | LEU347 |
| D | ASP400 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IOD C 627 |
| Chain | Residue |
| C | GLU514 |
| C | HOH701 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IOD D 628 |
| Chain | Residue |
| D | LYS323 |
| D | ASN324 |
| D | IOD604 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKsdNILL |
| Chain | Residue | Details |
| C | VAL385-LEU397 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by OXSR1","evidences":[{"source":"UniProtKB","id":"P35465","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"17989089","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"20417602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by JAK2","evidences":[{"source":"PubMed","id":"17726028","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17989089","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis, BRSK2 and PDPK1","evidences":[{"source":"PubMed","id":"10551809","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10995762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22153498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22669945","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP393 | |
| C | ASP389 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP393 | |
| D | ASP389 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS391 | |
| C | ASP389 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS391 | |
| D | ASP389 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS391 | |
| C | ASP389 | |
| C | THR427 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS391 | |
| D | ASP389 | |
| D | THR427 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | LYS391 | |
| C | ASP389 | |
| C | ASN394 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | LYS391 | |
| D | ASP389 | |
| D | ASN394 |
