eF-site/Summary 1fpg-A

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

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Title	STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
Classification	HYDROLASE (PHOSPHORIC MONOESTER)
Compound	FRUCTOSE 1,6-BISPHOSPHATASE
Source	Sus scrofa (Pig) (F16P_PIG)

Sequence	A:	NIVTLTRFVMEQGRKARGTGEMTQLLNSLCTAVKAISTAV RKAGIAHLYGIAGKLDVLSNDLVINVLKSSFATCVLVTEE DKNAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGI YRKNSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMV NGVNCFMLDPAIGEFILVDRNVKIKKKGSIYSINEGYAKE FDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTG KEAVLDIVPTDIHQRAPIILGSPEDVTELLEIYQKHA

Description	(1)	FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE, AND MN2+ (CONCENTRATION OF 300 MICROMOLAR)

Functional site


1)	chain	A
	residue	20
	type
	sequence	Q
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

2)	chain	A
	residue	17
	type
	sequence	V
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

3)	chain	A
	residue	31
	type
	sequence	T
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

4)	chain	A
	residue	140
	type
	sequence	R
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

5)	chain	A
	residue	113
	type
	sequence	Y
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

6)	chain	A
	residue	29
	type
	sequence	E
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

7)	chain	A
	residue	30
	type
	sequence	M
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

8)	chain	A
	residue	27
	type
	sequence	T
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

9)	chain	A
	residue	112
	type
	sequence	K
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

10)	chain	A
	residue	177
	type
	sequence	M
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

11)	chain	A
	residue	24
	type
	sequence	A
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

12)	chain	A
	residue	21
	type
	sequence	G
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

13)	chain	A
	residue	26
	type
	sequence	G
	description	AMP BINDING SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AM1

14)	chain	A
	residue	244
	type
	sequence	Y
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

15)	chain	A
	residue	212
	type
	sequence	N
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

16)	chain	A
	residue	215
	type
	sequence	Y
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

17)	chain	A
	residue	264
	type
	sequence	Y
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

18)	chain	A
	residue	274
	type
	sequence	K
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

19)	chain	A
	residue	248
	type
	sequence	M
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

20)	chain	A
	residue	276
	type
	sequence	R
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

21)	chain	A
	residue	280
	type
	sequence	E
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

22)	chain	A
	residue	122
	type
	sequence	G
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

23)	chain	A
	residue	121
	type
	sequence	D
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN A
	source	: AC1

24)	chain	A
	residue	243
	type
	sequence	R
	description	ACTIVE SITE IN MONOMER COMPOSED OF CHAIN B
	source	: AC2

25)	chain	A
	residue	97
	type
	sequence	E
	description	FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA1

26)	chain	A
	residue	118
	type
	sequence	D
	description	FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA1

27)	chain	A
	residue	280
	type
	sequence	E
	description	FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA1

28)	chain	A
	residue	121
	type
	sequence	D
	description	FIRST METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA1

29)	chain	A
	residue	97
	type
	sequence	E
	description	SECOND METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA3

30)	chain	A
	residue	118
	type
	sequence	D
	description	SECOND METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA3

31)	chain	A
	residue	120
	type
	sequence	L
	description	SECOND METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA3

32)	chain	A
	residue	98
	type
	sequence	E
	description	SECOND METAL SITE IN MONOMER COMPOSED OF CHAIN A
	source	: MA3

33)	chain	A
	residue	75
	type	catalytic
	sequence	V
	description	546
	source	MCSA : MCSA1

34)	chain	A
	residue	98
	type	catalytic
	sequence	E
	description	546
	source	MCSA : MCSA1

35)	chain	A
	residue	99
	type	catalytic
	sequence	D
	description	546
	source	MCSA : MCSA1

36)	chain	A
	residue	119
	type	catalytic
	sequence	P
	description	546
	source	MCSA : MCSA1

37)	chain	A
	residue	121
	type	catalytic
	sequence	D
	description	546
	source	MCSA : MCSA1

38)	chain	A
	residue	122
	type	catalytic
	sequence	G
	description	546
	source	MCSA : MCSA1

39)	chain	A
	residue	281
	type	catalytic
	sequence	C
	description	546
	source	MCSA : MCSA1

40)	chain	A
	residue	273-285
	type	prosite
	sequence	GKLRLLYECNPMA
	description	FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA
	source	prosite : PS00124

41)	chain	A
	residue	18
	type	BINDING
	sequence	M
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPD, ECO:0007744\|PDB:1FPE, ECO:0007744\|PDB:1FPF, ECO:0007744\|PDB:1FPG, ECO:0007744\|PDB:1FPI, ECO:0007744\|PDB:1FPJ, ECO:0007744\|PDB:1FPL, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP
	source	Swiss-Prot : SWS_FT_FI1

42)	chain	A
	residue	28
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPD, ECO:0007744\|PDB:1FPE, ECO:0007744\|PDB:1FPF, ECO:0007744\|PDB:1FPG, ECO:0007744\|PDB:1FPI, ECO:0007744\|PDB:1FPJ, ECO:0007744\|PDB:1FPL, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP
	source	Swiss-Prot : SWS_FT_FI1

43)	chain	A
	residue	113
	type	BINDING
	sequence	Y
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPD, ECO:0007744\|PDB:1FPE, ECO:0007744\|PDB:1FPF, ECO:0007744\|PDB:1FPG, ECO:0007744\|PDB:1FPI, ECO:0007744\|PDB:1FPJ, ECO:0007744\|PDB:1FPL, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP
	source	Swiss-Prot : SWS_FT_FI1

44)	chain	A
	residue	216
	type	MOD_RES
	sequence	A
	description	Phosphotyrosine => ECO:0000250\|UniProtKB:Q9QXD6
	source	Swiss-Prot : SWS_FT_FI10

45)	chain	A
	residue	245
	type	MOD_RES
	sequence	V
	description	Phosphotyrosine => ECO:0000250\|UniProtKB:Q9QXD6
	source	Swiss-Prot : SWS_FT_FI10

46)	chain	A
	residue	265
	type	MOD_RES
	sequence	P
	description	Phosphotyrosine => ECO:0000250\|UniProtKB:P09467
	source	Swiss-Prot : SWS_FT_FI11

47)	chain	A
	residue	98
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

48)	chain	A
	residue	119
	type	BINDING
	sequence	P
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

49)	chain	A
	residue	121
	type	BINDING
	sequence	D
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

50)	chain	A
	residue	122
	type	BINDING
	sequence	G
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

51)	chain	A
	residue	141
	type	BINDING
	sequence	K
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

52)	chain	A
	residue	281
	type	BINDING
	sequence	C
	description	BINDING => ECO:0000269\|PubMed:2164670
	source	Swiss-Prot : SWS_FT_FI2

53)	chain	A
	residue	213
	type	BINDING
	sequence	E
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:2QVU, ECO:0007744\|PDB:2QVV, ECO:0007744\|PDB:3FBP, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWU, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP
	source	Swiss-Prot : SWS_FT_FI3

54)	chain	A
	residue	244
	type	BINDING
	sequence	Y
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP
	source	Swiss-Prot : SWS_FT_FI4

55)	chain	A
	residue	265
	type	BINDING
	sequence	P
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FPB, ECO:0007744\|PDB:1FRP, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV6, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:2QVU, ECO:0007744\|PDB:2QVV, ECO:0007744\|PDB:4GBV, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWU, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWY, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP
	source	Swiss-Prot : SWS_FT_FI5

56)	chain	A
	residue	275
	type	BINDING
	sequence	L
	description	BINDING => ECO:0000269\|PubMed:10913263, ECO:0000269\|PubMed:12595528, ECO:0000269\|PubMed:1312721, ECO:0000269\|PubMed:14530289, ECO:0000269\|PubMed:15767255, ECO:0000269\|PubMed:17933867, ECO:0000269\|PubMed:1849642, ECO:0000269\|PubMed:2157849, ECO:0000269\|PubMed:2164670, ECO:0007744\|PDB:1CNQ, ECO:0007744\|PDB:1EYI, ECO:0007744\|PDB:1EYJ, ECO:0007744\|PDB:1EYK, ECO:0007744\|PDB:1FBP, ECO:0007744\|PDB:1FJ6, ECO:0007744\|PDB:1FJ9, ECO:0007744\|PDB:1FSA, ECO:0007744\|PDB:1KZ8, ECO:0007744\|PDB:1LEV, ECO:0007744\|PDB:1NUW, ECO:0007744\|PDB:1NUX, ECO:0007744\|PDB:1NUY, ECO:0007744\|PDB:1NUZ, ECO:0007744\|PDB:1NV0, ECO:0007744\|PDB:1NV1, ECO:0007744\|PDB:1NV2, ECO:0007744\|PDB:1NV3, ECO:0007744\|PDB:1NV4, ECO:0007744\|PDB:1NV5, ECO:0007744\|PDB:1NV7, ECO:0007744\|PDB:1Q9D, ECO:0007744\|PDB:1RDY, ECO:0007744\|PDB:1RDZ, ECO:0007744\|PDB:1YXI, ECO:0007744\|PDB:1YYZ, ECO:0007744\|PDB:1YZ0, ECO:0007744\|PDB:2F3B, ECO:0007744\|PDB:2F3D, ECO:0007744\|PDB:4GBW, ECO:0007744\|PDB:4GWS, ECO:0007744\|PDB:4GWW, ECO:0007744\|PDB:4GWX, ECO:0007744\|PDB:4GWZ, ECO:0007744\|PDB:4GX3, ECO:0007744\|PDB:4GX4, ECO:0007744\|PDB:4GX6, ECO:0007744\|PDB:4H45, ECO:0007744\|PDB:4H46, ECO:0007744\|PDB:4KXP, ECO:0007744\|PDB:5FBP
	source	Swiss-Prot : SWS_FT_FI6

57)	chain	A
	residue	151
	type	MOD_RES
	sequence	D
	description	N6-succinyllysine => ECO:0000250\|UniProtKB:Q9QXD6
	source	Swiss-Prot : SWS_FT_FI8

58)	chain	A
	residue	208
	type	MOD_RES
	sequence	I
	description	Phosphoserine; by PKA => ECO:0000269\|PubMed:6296821
	source	Swiss-Prot : SWS_FT_FI9