eF-site ID 1ny3-A
PDB Code 1ny3
Chain A

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Title Crystal structure of ADP bound to MAP KAP kinase 2
Classification TRANSFERASE
Compound MAP kinase-activated protein kinase 2
Source Homo sapiens (Human) (MAPK2_HUMAN)
Sequence A:  FHVKSGLQIKKNAIIDDYKVTSQVLGLGINGKVLQIFNKR
TQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVYE
NLYAGRKCLLIVMECLDGGELFSRIQDTEREASEIMKSIG
EAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFA
KETTSHPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGY
PPFYSGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKT
EPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKED
Description


Functional site

1) chain A
residue 70
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

2) chain A
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

3) chain A
residue 72
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

4) chain A
residue 73
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

5) chain A
residue 74
type
sequence I
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

6) chain A
residue 91
type
sequence A
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

7) chain A
residue 93
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

8) chain A
residue 139
type
sequence E
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

9) chain A
residue 141
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

10) chain A
residue 191
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

11) chain A
residue 207
type
sequence D
description BINDING SITE FOR RESIDUE ADP A 401
source : AC1

12) chain A
residue 70-93
type prosite
sequence LGLGINGKVLQIFNKRTQEKFALK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK
source prosite : PS00107

13) chain A
residue 182-194
type prosite
sequence IAHRDVKPENLLY
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY
source prosite : PS00108

14) chain A
residue 186
type ACT_SITE
sequence D
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 70
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 93
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 139
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 328
type MOD_RES
sequence S
description Phosphoserine; by autocatalysis => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

19) chain A
residue 334
type MOD_RES
sequence T
description Phosphothreonine; by MAPK14 => ECO:0000269|PubMed:8846784, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


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