2J0J

PTK2 (Focal adhesion kinase 1)
Group: TYR
Uniprot: FAK1_CHICK
Organism: Gallus gallus
Domain boundary: 422 - 678
Resolu: 2.8

Chain id Activity_label Spatial_label Dihedral_label Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop
A Inactive DFGin None in-in out-out 4ST Type1 35 - 686 10
Representative sequence - Chain A
40 50 60 70
gameRVLKVF HYFENSSEPT TWASIIRHGD ATDVRGIIQK
80 90 100 110
IVDCHKVKNV ACYGLRLSHL QSEEVHWLHL DMGVSNVREK
120 130 140 150
FELAHPPEEW KYELRIRYLP KGFLNQFTED KPTLNFFYQQ
160 170 180 190
VKNDYMLEIA DQVDQEIALK LGCLEIRRSY GEMRGNALEK
200 210 220 230
KSNYEVLEKD VGLRRFFPKS LLDSVKAKTL RKLIQQTFRQ
240 250 260 270
FANLNREESI LKFFEILSPV YRFDKECFKC ALGSSWIISV
280 290 300 310
ELAIGPEEGI SYLTDKGANP THLADFNQVQ TIQYSNSEDK
320 330 340 350
DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL
360 370 380 390
VNGATQSFII RPqkegeral psipklanne kqgvrshtvs
400 410 420 430
vseTDDYAEI IDEEDTYTMP STRDYEIQRE RIELGRCIGE
440 450 460 470
GQFGDVHQGI YMSPENPAMA VAIKTCKNCT SDSVREKFLQ
480 490 500 510
EALTMRQFDH PHIVKLIGVI TENPVWIIME LCTLGELRSF
520 530 540 550
LQVRKFSLDL ASLILYAYQL STALAYLESK RFVHRDIAAR
560 570 580 590
NVLVSSNDCV KLGDFGLSRY MEDstyykas kgkLPIKWMA
600 610 620 630
PESINFRRFT SASDVWMFGV CMWEILMHGV KPFQGVKNND
640 650 660 670
VIGRIENGER LPMPPNCPPT LYSLMTKCWA YDPSRRPRFT
680
ELKAQLSTIL EEEKLQ
Lower-case residues are disordered in structure.
Mutations: None
Phosphorylation: None