eF-site/Summary 4g1m-B

eF-site ID	4g1m-B
PDB Code	4g1m
Chain	B

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Title	Re-refinement of alpha V beta 3 structure
Classification	PROTEIN BINDING
Compound	Integrin alpha-V
Source	(ITB3_HUMAN)

Sequence	B:	GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDL KENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDL SYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQV TRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNH YSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVR DLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQ AEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKY CECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEK CPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILY VVEEPECPKGPD

Description	(1)	Integrin alpha-V, Integrin beta-3

Functional site


1)	chain	B
	residue	460-471
	type	prosite
	sequence	CRCGPGWLGSQC
	description	EGF_1 EGF-like domain signature 1. CrCgpGwlGSqC
	source	prosite : PS00022

2)	chain	B
	residue	547-558
	type	prosite
	sequence	CLCDSDWTGYYC
	description	EGF_1 EGF-like domain signature 1. CrCgpGwlGSqC
	source	prosite : PS00022

3)	chain	B
	residue	495-508
	type	prosite
	sequence	CSQRGECLCGQCVC
	description	INTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsQr..GeClCgqCvC
	source	prosite : PS00243

4)	chain	B
	residue	536-549
	type	prosite
	sequence	CSGHGQCSCGDCLC
	description	INTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsQr..GeClCgqCvC
	source	prosite : PS00243

5)	chain	B
	residue	575-588
	type	prosite
	sequence	CSGRGKCECGSCVC
	description	INTEGRIN_BETA Integrins beta chain cysteine-rich domain signature. CsQr..GeClCgqCvC
	source	prosite : PS00243

6)	chain	B
	residue	460-473
	type	prosite
	sequence	CRCGPGWLGSQCEC
	description	EGF_2 EGF-like domain signature 2. CrCgpGWlgsqce..C
	source	prosite : PS01186

7)	chain	B
	residue	1-692
	type	TOPO_DOM
	sequence	GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDL KENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQV TQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDL SYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKP VSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQV TRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRN DASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNH YSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQN YSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVR DLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIE AKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQ AEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRP SQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKY CECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNC TTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEK CPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIE SVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILY VVEEPECPKGPD
	description	Extracellular => ECO:0000255
	source	Swiss-Prot : SWS_FT_FI1

8)	chain	B
	residue	452
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI10

9)	chain	B
	residue	559
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI11

10)	chain	B
	residue	654
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:19159218, ECO:0007744\|PDB:1JV2
	source	Swiss-Prot : SWS_FT_FI12

11)	chain	B
	residue	121
	type	BINDING
	sequence	S
	description	in MIDAS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI2

12)	chain	B
	residue	220
	type	BINDING
	sequence	E
	description	in MIDAS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI2

13)	chain	B
	residue	123
	type	BINDING
	sequence	S
	description	in MIDAS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI3

14)	chain	B
	residue	126
	type	BINDING
	sequence	D
	description	in ADMIDAS binding site => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI4

15)	chain	B
	residue	127
	type	BINDING
	sequence	D
	description	in ADMIDAS binding site => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI4

16)	chain	B
	residue	158
	type	BINDING
	sequence	D
	description	in LIMBS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI5

17)	chain	B
	residue	215
	type	BINDING
	sequence	N
	description	in LIMBS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI5

18)	chain	B
	residue	217
	type	BINDING
	sequence	D
	description	in LIMBS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI5

19)	chain	B
	residue	219
	type	BINDING
	sequence	P
	description	in LIMBS binding site => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3FCU
	source	Swiss-Prot : SWS_FT_FI5

20)	chain	B
	residue	251
	type	BINDING
	sequence	D
	description	in LIMBS binding site => ECO:0007744\|PDB:4G1M
	source	Swiss-Prot : SWS_FT_FI6

21)	chain	B
	residue	335
	type	BINDING
	sequence	M
	description	in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:3FCS, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI7

22)	chain	B
	residue	99
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:16263699, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI8

23)	chain	B
	residue	320
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI9

24)	chain	B
	residue	371
	type	CARBOHYD
	sequence	N
	description	N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:11546839, ECO:0000269\|PubMed:15378069, ECO:0000269\|PubMed:19111664, ECO:0000269\|PubMed:19704023, ECO:0007744\|PDB:1JV2, ECO:0007744\|PDB:1TYE, ECO:0007744\|PDB:3IJE
	source	Swiss-Prot : SWS_FT_FI9