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 |